Röntgenstrahlen in der Biochemie

  • Peter Reinemer
  • Robert Huber
Chapter

Zusammenfassung

Von ihren Anfängen an ist es ein Erfolgskonzept der Biochemie gewesen, die biologischen Funktionen auf der Basis chemischer Strukturen zu erklären. So ist unser heutiges Verständnis der Lebenserscheinungen nachhaltig von den Strukturaufklärungen biochemisch relevanter Moleküle beeinflußt worden. Dies gilt insbesondere für die Makromoleküle, die die zentralen Träger biologischer Information und Funktion sind: die Nukleinsäuren und Proteine. Ganz offensichtlich ist die Entschlüsselung ihres Aufbaus notwendige Voraussetzung für das Verständnis ihrer Funktion; M. Perutz schrieb dazu mit Blick auf die Enzyme, einer Klasse von Proteinen, die als biologische Katalysatoren in allen biochemischen Prozessen mitwirken:

„Um die chemischen Grundlagen des Lebens verstehen zu können, müssen wir den Apparat kennen, der komplizierte Pflanzen und Tiere aus einfachen chemischen Verbindungen aufbaut. Welche Werkzeuge besitzen lebende Zellen, um große organische Moleküle in wässrigem Medium bei normalen Temperaturen und in neutraler Lösung aufzubauen, ein Vorhaben, für das der Chemiker wirksame Lösungsmittel, hohe Temperaturen, niedrige Drücke und starke Säuren oder Basen braucht?“ (Perutz 1971).

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Literatur

  1. Adams MJ, Blundell TL, Dodson EJ et al. (1969) Structure of rhombohedral 2 zinc insulin crystals. Nature 224:491–495.CrossRefGoogle Scholar
  2. Adams MJ, Ford GC, Koekoek R et al. (1970) Structure of lactate dehydrogenase at 2,8 Å resolution. Nature 227:1098–1103.PubMedCrossRefGoogle Scholar
  3. Albrecht G, Corey RB (1939) The crystal structure of glycine. J Am Chem Soc 61:1087–1103.CrossRefGoogle Scholar
  4. Astbury WT (1931) X-ray investigations of the inner structure of wool. J Textile Sci 4:1–5.Google Scholar
  5. Astbury WT (1933) Fundamentals of fibre structure. Oxford University Press, New York.Google Scholar
  6. Astbury WT (1961) Molecular biology or ultrastructural biology? Nature 190:1124.PubMedCrossRefGoogle Scholar
  7. Astbury WT, Bell FC (1938) X-ray study of thymonucleic acid. Nature 141:747–748.CrossRefGoogle Scholar
  8. Astbury WT, Bell FC (1941) Nature of the intramolecular fold in α-keratin and α-myosin. Nature 147:696–699.CrossRefGoogle Scholar
  9. Astbury WT, Sisson WA (1935) X-ray studies of the structures of hair, wool and related fibers. III. The configuration of the keratin molecule and its orientation in the biological cell. Proc Roy Soc (London) A 150:333–351.CrossRefGoogle Scholar
  10. Astbury WT, Street A (1931) X-ray studies of the structure of hair, wool and related fibers. I. General. Trans Roy Soc (London) A230:75–101.Google Scholar
  11. Astbury WT, Woods JH (1930) The X-ray interpretation of the structure and elastic properties of hair keratin. Nature 126:913–914.CrossRefGoogle Scholar
  12. Astbury WT, Woods HJ (1931) Moiecular weights of proteins. Nature 127:663–665.CrossRefGoogle Scholar
  13. Astbury WT, Woods HJ (1934) X-ray studies of the structure of hair, wool and related fibers. II, The molecular structure and elastic properties of hair keratin. Trans Roy Soc (London) A232:333–394.CrossRefGoogle Scholar
  14. Astbury WT, Dickinson S, Bailey K (1935) The X-ray interpretation of denaturation and the structure of the seed globulin. Biochem J 29:2351–2361.PubMedGoogle Scholar
  15. Avery OT, MacLeod CM, MacCarty M (1944) Studies on the chemical nature of the substance inducing transformation of pneumococcal types. J Exp Med 79:137–158.PubMedCrossRefGoogle Scholar
  16. Baldwin J, Chothia C (1979) Haemoglobin: The structural changes related to binding and its allosteric mechanism. J Mol Biol 129:175–220.PubMedCrossRefGoogle Scholar
  17. Bamford CH, Brown L, Cant EM, Elliott A, Hanley WE, Malcolm BR (1955) Structure of polyglycine, Nature 176:396–397.CrossRefGoogle Scholar
  18. Baumann U, Shan W, Flaherty KM, McKay DB (1993) Three-dimensional structure of the alkaline protease of pseudomonas aemginosa: A two-domain protein with a calcium binding parallel beta roll motif. EMBO J 12:3357–3364.PubMedGoogle Scholar
  19. Baumgärtner KH (1830) Beobachtungen über die Nerven und das Blut. Freiburg.Google Scholar
  20. Bernal JD (1931) The crystal structure of natural amino acids and related compounds. Z Krist 78:363–369.Google Scholar
  21. Bernal JD, Crowfoot D (1934) X-ray photographs of crystalline pepsin. Nature 133:794–795.CrossRefGoogle Scholar
  22. Bernal JD, Fankuchen I (1941) X-ray and crystallographic studies of plant virus preparations. I. Introduction and preparation of specimens. II. Mode of aggregation of the virus particle. III. X-ray and crystaliographic studies of plant virus preparations. J Gen Physiol 25:111–165.PubMedCrossRefGoogle Scholar
  23. Bernai JD, Fankuchen I, Perutz MF (1938) X-ray study of chymotrypsin and hemoglobin. Nature 141:523–524.CrossRefGoogle Scholar
  24. Bernstein FC, Koetzle TF, Williams GJB et al. (1977) The protein data bank: A computer-based archival file for macromolecular structures. J Mol Biol 112:535–542.PubMedCrossRefGoogle Scholar
  25. Bijvoet JM (1954) Structure of optically active compounds in the solid state. Nature 173:888–891.CrossRefGoogle Scholar
  26. Blake CCF, Koenig DF, Mair GA, North ACT, Phillips DC, Sarma VR (1965) Structure of hen egg-white lysozyme. A three-dimensional Fourier-synthesis at 2Å resolution. Nature 206:757–761.PubMedCrossRefGoogle Scholar
  27. Bloomer AC, Champness JN, Bricogne G, Staden R, Klug A (1978) Protein discs of tobacco mosaic virus at 2,8 Å resolution showing the interactions within and between subunits, Nature 276:362–368.PubMedCrossRefGoogle Scholar
  28. Blow DM (1958) The structure of haemoglobin. VII. Determination of phase angles in the noncentrosymmetric (100) zone. Proc Roy Soc (London) A247:302–336.Google Scholar
  29. Blow DM, Crick FHC (1959) The treatment of errors in the isomorphous replacement method. Acta Cryst 12:794–802.CrossRefGoogle Scholar
  30. Blow DM, Rossmann MG (1961) The single isomorphous replacement methode. Acta Cryst 14:1195–1202.CrossRefGoogle Scholar
  31. Blow DM, Birkroft JJ, Hartley BS (1969) Role of a buried acid group in the mechanism of action of chymotrypsin. Nature 221:337–340.PubMedCrossRefGoogle Scholar
  32. Blow DM, Janin J, Sweet RM (1974) Mode of action of soybean trypsin inhibitor (Kunitz) as a model for specific protein-protein-interactions. Nature 249:54–57.PubMedCrossRefGoogle Scholar
  33. Blow DM, Wright CS, Kukla D, Rühlmann A, Steigemann W, Huber R (1972) A model for the association of bovine pancreatic trypsin inhibitor with chymotrypsin and trypsin. J Mol Biol 69:137–144].PubMedCrossRefGoogle Scholar
  34. Bode W, Schwaer P (1975) The refined crystal structure of bovine ß-trypsin at 1,8 Å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0. J Mol Biol 98:693–717.PubMedCrossRefGoogle Scholar
  35. Bodo G, Dintzis HM, Kendrew JC, Wyckoff HW (1959) Crystal structure of myogiobin, V. Low-resolution three-dimensional Fourier synthesis of sperm whale myogiobin crystals, Proc Roy Soc (London) A253:70–102.Google Scholar
  36. Bolton W, Cox JM, Perutz MF (1968) Structure and function of haemoglobin IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5,5 Å resolution. J Mol Biol 33:283–297.PubMedCrossRefGoogle Scholar
  37. Bolton W, Perutz MF (1970) Three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 2,8 AÅresolution. Nature 228:551–552.PubMedCrossRefGoogle Scholar
  38. Bokhoven C, Schoone JC, Bijvoet JM (1949) On the crystal structure of strychnine sulfate and selenate. III. [001]-Projection. Proc Kgl Ned Akad Wet 52:120–121.Google Scholar
  39. Bokhoven C, Schoone JC, Bijvoet JM (1951) The Fourier synthesis of the crystal structure of strychnine sulfate pentahydrate. Acta Cryst 4:275–280.CrossRefGoogle Scholar
  40. Bragg WH (1915) IX. Bakerian Lecture: X-rays and crystal structures. Trans Roy Soc (London) A215:253–274.CrossRefGoogle Scholar
  41. Bragg WL, Perutz MF (1952a) The structure of hemoglobin. Proc Roy Soc (London) A213:425–435.Google Scholar
  42. Bragg WL, Perutz MF (1952b) The external form of the haemoglobin molecule. II, Acta Cryst 5:323–328.CrossRefGoogle Scholar
  43. Bragg WL, Perutz MF (1954) The structure of hemoglobin. VI. Fourier projections on the 010 plane. Proc Roy Soc (London) A225:315–329.Google Scholar
  44. Bragg WL, Kendrew JC, Perutz MF (1950) Polypeptide chain configurations in crystalline proteins. Proc Roy Soc (London) A203:321–357.Google Scholar
  45. Bricogne G (1976) Methods of programms for directspace exploitation of geometric-redundancies. Acta Cryst A32:832–847.Google Scholar
  46. Brill R (1923) Über Seidenfibroin. Liebigs Ann Chemie 434:204–217.CrossRefGoogle Scholar
  47. Brünger AT, Kuriyan J, Karpius M (1987) Crystaliographic R-factor refinement by moiecular dynamics. Science 235:458–460.PubMedCrossRefGoogle Scholar
  48. Brünger AT, Karplus M, Petsko GA (1989) Crystaliographic refinement by simulated annealing: Application to Crambin. Acta Cryst A45:50–61.Google Scholar
  49. Brünger AT, Krakowski A, Erikson J (1990) Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Cryst A46:585–593.Google Scholar
  50. Butler PJG, Klug A (1978) The assembly of a virus. Sci Am 239:62–69.PubMedGoogle Scholar
  51. Caspar DLD, Klug A (1962) Physical principles in the construction of regular viruses. Cold Spring Harbour Symp Quant Biol 27:1–24.CrossRefGoogle Scholar
  52. Chargaff E (1950) Chemical specificity of nucleic acids and mechanism of their enzymatic degradation. Experientia 6:201–209.PubMedCrossRefGoogle Scholar
  53. Cochran W (1951) The structures of pyrimidines and purines. V. The electron distribution in adenine hydrochloride. Acta Cryst 4:81–92.CrossRefGoogle Scholar
  54. Cochran W, Crick FHC, Vand V (1952) Structure of synthetic polypeptides. I. The transform of atoms on a helix. Acta Cryst 5:581–586.CrossRefGoogle Scholar
  55. Corey RB (1938) Crystal structure of diketopiperazine. J Am Chem Soc 60:1598–1604.CrossRefGoogle Scholar
  56. Cork JM (1927) Crystal structures of the alums. Phil Mag 4:688–698.Google Scholar
  57. Coster D, Knol KS, Prins JA (1930) Unterschiede in der Intensität der Röntgenstrahlenreflexion an den beiden 111-Flächen der Zinkblende. Z Phys 63:345–369.CrossRefGoogle Scholar
  58. Cowan PM, McGavin S (1955) Structure of Poly-L-proline. Nature 176:501–503.CrossRefGoogle Scholar
  59. Crick FHC (1953a) Is α-Keratin a coiled coil? Nature 170:882–883.CrossRefGoogle Scholar
  60. Crick FHC (1953b) The packing of α-helices: Simple coiled-coils. Acta Cryst 6:689–697.CrossRefGoogle Scholar
  61. Crick FHC, Magdoff BS (1956) The theory of the method of isomorphous replacement for protein crystals. I. Acta Cryst 9:901–908.CrossRefGoogle Scholar
  62. Crick FHC, Rich A (1955) Structure of polyglycine II. Nature 176:780–781.PubMedCrossRefGoogle Scholar
  63. Crick FHC, Watson JD (1956) Structure of small viruses. Nature 177:473–475.PubMedCrossRefGoogle Scholar
  64. Crowfoot D (1935) X-ray single crystal photographs of insulin. Nature 135:591–592.CrossRefGoogle Scholar
  65. Crowfoot-Hodgkin D (1979) Crystailographic measurements and the structure of protein molecules as they are. Ann N Y Acad Sci 325:121–145.CrossRefGoogle Scholar
  66. Crowfoot D, Riley DP (1938) X-ray study of Palmer’s lactoglobulin. Nature 141:521–522.CrossRefGoogle Scholar
  67. Crowfoot D, Riley DP (1939) X-ray measurements of wet insulin crystals. Nature 144:1011–1012.CrossRefGoogle Scholar
  68. Crowfoot-Hodgkin D, Riley DP (1968) Some ancient history of protein X-ray analysis, in: Rich A, Davidson N (eds) Structural chemistry and molecular biology. Freeman, San Francisco.Google Scholar
  69. Crowther RA, Blow DM (1967) A method of positioning a know molecule in an unknown crystal structure. Acta Cryst 23:544–548.CrossRefGoogle Scholar
  70. Cullis AF, Muirhead H, Perutz MF, Rossmann MG, North ACT (1961a) Structure of haemoglobin. VIII. A three-dimensional Fourier synthesis at 5,5 Å resolution. Determination of phase angles. Proc Roy Soc (London) A265:15–38.Google Scholar
  71. Cullis AF, Muirhead H, Perutz MF, Rossmann MG, North ACT (1961b) Structure of haemoglobin. IX. A Three-dimensional Fourier synthesis at 5,5 resolution: Description of the structure. Proc Roy Soc (London) A 265:161–387.CrossRefGoogle Scholar
  72. Deisenhofer J, Epp O, Miki K, Huber R, Michel H (1984) X-ray structure analysis of a membrane protein complex: Electron density map at 3 Ä resolution and a model of the chromophores of the photosynthetic reaction center from rhodopseudomonas viridis. J Mol Biol 180:385–398.PubMedCrossRefGoogle Scholar
  73. Deisenhofer J, Epp O, Miki K, Huber R, Michel H (1985) Structure of the protein subunits in the photosynthetic reaction centre of rhodopseudomonas viridis at 3 A Resolution. Nature 318:618–624.CrossRefGoogle Scholar
  74. Diamond R (1971) A real-space refinement procedure for proteins. Acta Cryst A 27:436–452.CrossRefGoogle Scholar
  75. Dickerson RE, Kendrew JC, Strandberg BE (1961) The crystal structure of myoglobin: Phase determination to a resolution of 2 Å by the method of isomorphous replacement. Acta Cryst 14:1188–3195.CrossRefGoogle Scholar
  76. Donohue J (1953) Hydrogen-bonded helical configurations of the poiypeptide chain. Proc Natl Acad Sci USA 39:470–478.PubMedCrossRefGoogle Scholar
  77. Drenth J, Jansonius JN, Koekoek R, Swen HM, Wolthers BG (1968) Structure of papain. Nature 218:929–932.PubMedCrossRefGoogle Scholar
  78. Drenth J, Hol WG, Jansonius JN, Kroekoek R (1971) A comparison of the three-dimensional structures of Subtilisin BPN’ and Subtilisin Novo. Cold Spring Harbour Symp Quant Biol 36:107–116.CrossRefGoogle Scholar
  79. Duane W (1925) The calculation of the X-ray diffraction power at points in a crystal. Proc Natl Acad Sci USA 11:489–493.PubMedCrossRefGoogle Scholar
  80. Ealick SE, Walter RL (1993) Synchrotron beamlines for macromolecular crystallography. Curr Opin Struct Biol 3:725–736.CrossRefGoogle Scholar
  81. Fehthammer H, Bode W (1975) The refined crystal structure of bovine β-trypsin at 1,8 Å resolution. I. Crystallization, data collection and application of Patterson search techniques. J Mol Biol 98:683–692.CrossRefGoogle Scholar
  82. Finzel BC (1993) Software for macromolecular crystallography: A user’s overview. Curr Opin Struct Biol 3:741–747.CrossRefGoogle Scholar
  83. Forest K, Schutt C (1992) Protein engineering for structure determination. Curr Opin Struct Biol 2:576–581.CrossRefGoogle Scholar
  84. Franklin RE, Gosling RG (1953a) The structure of sodium thymonucleate fibers. I. The influence of water content. Acta Cryst 6:673–677.CrossRefGoogle Scholar
  85. Franklin RE, Gosling RG (1953b) The structure of sodium thymonucleate fibers. II. The cylindrically symmetrical Patterson-function. Acta Cryst 6:678–685.CrossRefGoogle Scholar
  86. Franklin RE, Gosling RG (1953c) Molecular configuration of sodium thymonucleate. Nature 171:740–741.PubMedCrossRefGoogle Scholar
  87. Franklin RE, Gosling RG (1953d) Evindence for 2-chain helix in crystalline structure of sodium desoxyribonucleate. Nature 172:356–357.CrossRefGoogle Scholar
  88. Franklin RE, Gosling RG (1955) The structure of sodium thymonucleate fibers. III. The three-dimensional Patterson function. Acta Cryst 8:151–156.CrossRefGoogle Scholar
  89. Freer ST, Kraut J, Robertus JD, Wright HT, Xuong NH (1970) Chymotrypsinogen: 2,5 Å crystal structure, comparison with α-chymotrypsin, and implications for zymogen activation. Biochemistry 9:1997–2009.PubMedCrossRefGoogle Scholar
  90. Freer ST, Alden RA, Carter CW, Kraut J (1975) Crystallographic structure refinement of chromatin high potential protein at 2 A resolution. J Biol Chem 250:46–54.PubMedGoogle Scholar
  91. Friedel G (1913) Sur les symétries cristallines que peut reveler la diffraction des rayons Röntgen. Compt Rend 157:1533–1536.Google Scholar
  92. Friedrich W, Knipping P, Laue M (1912) Interferenz-Erscheinungen bei Röntgenstrahlen. Sitzungsber Kgl Bayer Akad Wiss 303-322.Google Scholar
  93. Fujinaga M, Gros P, van Gunsteren WF (1989) Testing the method of crystallographic refinement using molecular dynamics. J Appl Cryst 22:1–8.CrossRefGoogle Scholar
  94. Furberg S (1949a) Crystal structure of cytidine. Nature 164:22.PubMedCrossRefGoogle Scholar
  95. Furberg S (1949b) An X-ray study of some nucleosides and nucleotides. Dissertation, Universität London.Google Scholar
  96. Furberg S (1950a) The crystal structure of cytidine. Acta Cryst 3:325–333.CrossRefGoogle Scholar
  97. Furberg S (1950b) X-ray studies on the decomposition products of the nucleic acids. J Chem Soc Faraday Trans 46:791.Google Scholar
  98. Furberg S (1952) On the structure of nucleic acids. Acta Chem Scand 6:634–640.CrossRefGoogle Scholar
  99. Green DW, Ingram VM, Perutz MF (1954) The structure of haemoglobin. IV. Sign determination by the isomorphous replacement method. Proc Roy Soc (London) A225:287–307.Google Scholar
  100. Gulland JM, Jordan DO, Taylor HFW (1947) Desoxypentose nucleic acids. II. Electrometric titration of the acidic and basic groups of the desoxypentose nucleic acid of calf thymus. J Chem Soc 1131-1141.Google Scholar
  101. Gurskaya GV (1968) The molecular structure of amino acids. Determination by X-ray diffraction analysis. Consultants Bureau, New York.Google Scholar
  102. Harding MM, Crowfoot-Hodgkin DC, Kennedy AF, O’Connor A, Weitzmann PDJ (1966) The crystal structure of insulin. II. An investigation of rhombohedral zinc insulin crystals and a report of other crystalline forms. J Mol Biol 16:212–226.PubMedCrossRefGoogle Scholar
  103. Harker D (1936) The application of the three-dimensional Patterson method and the crystal structure of prousite Ag3AsS3, and pyrargyrite, Ag3SbS3. J Chem Phys 4:381–390.CrossRefGoogle Scholar
  104. Harker D (1956) The determination of the phases of the structure factors of non-centrosymmetric crystals by the method of double isomorphous replacement. Acta Cryst 9:1–9.CrossRefGoogle Scholar
  105. Harrington CR, Neuberger A (1936) Electrometric titration of insulin. Preparation and properties of iodinated insulin. Biochem J 30:809–820.Google Scholar
  106. Harrison SC (1968) A point-focussing camera for singlecrystal diffraction. J Appl Cryst 1:84–90.CrossRefGoogle Scholar
  107. Harrison SC, Olson AJ, Schutt CE, Winkler FK, Bricogne G (1978) Tomato bushy stunt virus at 2,9 Å resolution. Nature 276:368–373.PubMedCrossRefGoogle Scholar
  108. Hartsuck JA, Ludwig ML, Muirhead H, Steitz TA, Lipscomb WN (1965) Carboxypeptidase A. II. The three-dimensional electron density map at 6 Å resolution. Proc Natl Acad Sci USA 53:396–403.PubMedCrossRefGoogle Scholar
  109. Havighurst RJ (1926) Parameters in crystal structure. The mercurous halides. J Am Chem Soc 48:2113–2125.CrossRefGoogle Scholar
  110. Henderson R (1970) Structure of crystalline α-chymotrypsin. IV. The structure of indoleacryloyl-α-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme. J Mol Biol 54:341–354.PubMedCrossRefGoogle Scholar
  111. Henderson R, Wright CS, Hess GP, Blow DM (1971) α-Chymotrypsin: What can we learn about catalysis from X-ray diffraction. Cold Spring Harbour Symp Quant Biol 36:63–70.CrossRefGoogle Scholar
  112. Hendrickson WA, Lattmann EE (1970) Representation of phase probability distributions for simplified combination of independent phase information. Acta Cryst B26:136–143.Google Scholar
  113. Hendrickson WA (1985) Stereochemically restrained refinement of macromolecuiar structures. Meth Enzymol 115:252–270.PubMedCrossRefGoogle Scholar
  114. Hendrickson WA (1991) Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254:51–58.PubMedCrossRefGoogle Scholar
  115. Herriott JR, Sicker LC, Jensen LH, Lovensberg W (1970) Structure of rubredoxin: An X-ray study to 2,5 Å resolution. J Moi Biol 50:391–406.CrossRefGoogle Scholar
  116. Hershey AD, Chase M (1952) Independent functions of viral protein and nucleic acid in growth of bacteriophage. J Gen Physiol 36:39–56.PubMedCrossRefGoogle Scholar
  117. Herzog RO, Jahncke W (1920) Über den physikalischen Aufbau einiger hochmolekularer organischer Verbindungen. Ber Dtsch Chem Ges 53:2162–2164.CrossRefGoogle Scholar
  118. Hoppe W (1957a) Die Faltmolekülmethode: eine neue Methode zur Bestimmung der Kristallstruktur bei ganz oder teilweise bekannten Molekülstrukturen. Acta Cryst 10:750–751.Google Scholar
  119. Hoppe W (1957b) Die Faltmolekülmethode und ihre Anwendung in der röntgenographischen Konstitutionsanalyse von Biflorin (C20H20O4). Z Elektrochem 61:1076–1083.Google Scholar
  120. Hoppe W (1959) Die Bestimmung genauer Schweratomparameter in isomorphen azentrischen Kristallen. Acta Cryst 12:665–674.CrossRefGoogle Scholar
  121. Hönl H (1933) Zur Dispersionstheorie der Röntgenstrahlen. Z Phys 84:1–16.CrossRefGoogle Scholar
  122. Huber R (1965) Die automatisierte Faltmolekülmethode. Acta Cryst 19:353–356.CrossRefGoogle Scholar
  123. Huber R, Epp O, Formanek H (1969) Aufklärung der Molekülstruktur des Insekten-Hämoglobins. Naturwissenschaften 56:362–367.PubMedCrossRefGoogle Scholar
  124. Huber R, Kukla D, Rühlmann A, Epp O, Formanek H (1970) The basic trypsin inhibitor of bovine pancreas. I. Structure analysis and conformation of the poiypeptide chain. Naturwissenschaften 57:389–392.PubMedCrossRefGoogle Scholar
  125. Huber R, Kukla D, Bode W, Schwager P, Bartels K, Deisenhofer J, Steigemann W (1974) Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1, 9 Å resolution. J Mol Biol 89:73–101.PubMedCrossRefGoogle Scholar
  126. Huggins ML (1940) Some hydrogen-bridge modells for globular proteins. J Chem Phys 8:598–600.CrossRefGoogle Scholar
  127. Huggins ML (1943) The structure of fibrous proteins. Chem Rev 32:195–218.CrossRefGoogle Scholar
  128. Hughes EW, Moore WJ (1949) The crystal structure of α-glycylglycine. J Am Chem Soc 71:2618–2623.CrossRefGoogle Scholar
  129. Jack A, Levitt MA (1978) Refinement of large structures by simultaneous minimization of energy and R-factor. Acta Cryst A34:931–935.Google Scholar
  130. Jones TA (1978) A graphics model building and refinement system for macromolecules. J Appl Cryst 11:268–272.CrossRefGoogle Scholar
  131. Kallmann H, Mark H (1927) Über die Dispersion und Streuung von Röntgenstrahlen. Ann Phys 82:585–604.CrossRefGoogle Scholar
  132. Kartha G, Parthasarathy R (1965a) Combination of multiple isomorphous replacement and anomalous dispersion data for protein structure determination. I. Determination of heavy atom positions in protein derivatives. Acta Cryst 18:745–749.CrossRefGoogle Scholar
  133. Kartha G, Parthasarathy R (1965b) Combination of multiple isomorphous replacement and anomalous dispersion data for protein structure determination. II. Correlation of the heavy-atom positions in different isomorphous protein crystals. Acta Cryst 18:749–753.CrossRefGoogle Scholar
  134. Kartha G, Bello J, Harker D (1967) Tertiary structure of ribonuclease. Nature 213:862–865.PubMedCrossRefGoogle Scholar
  135. Kendrew JC (1948) Preliminary X-ray data for horse and whale myoglobins. Acta Cryst 1:336.CrossRefGoogle Scholar
  136. Kendrew JC (1954) The crystalline proteins: Recent X-Ray studies and structural hypotheses. Prog Biophys Biophys Chem 4:244–287.Google Scholar
  137. Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H (1958) A three-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 181:662–666.PubMedCrossRefGoogle Scholar
  138. Kendrew JC, Dickerson RE, Strandberg BE, Hart RG, Davis DR (1960) Structure of myoglobin. A three-dimensional Fourier synthesis at 2 Å resolution. Nature 185:422–427.PubMedCrossRefGoogle Scholar
  139. Konnert H (1976) A restrained-parameter structurefactor least-squares refinement procedure for large asymmetric units. Acta Crystr A32:614–617.CrossRefGoogle Scholar
  140. Koshland DE jr, Némethy G, Filmer D (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5:365–385.PubMedCrossRefGoogle Scholar
  141. Lipson H, Beevers CA (1935) The crystal structure of the alaums. Proc Roy Soc (London) A148:664–680.Google Scholar
  142. Lipson H, Beevers CA (1936) An improved numerical method of two-dimensional Fourier synthesis for crystals. Proc Phys Soc (London) 48:772–780.CrossRefGoogle Scholar
  143. Ludwig ML, Hartsuck JA, Steitz TA, Muirhead H, Coppola JC, Reeke GN, Lipscomb WN (1967) The structure of carboxypeptidase A, IV, Preliminary results at 2,8 Å resolution, and a substrate complex at 6Å resolution. Proc Natl Acad Sci USA 57:511–514.CrossRefGoogle Scholar
  144. Leung YC, Marsch RE (1958) The crystal structure of L-leucyl-L-prolyl-glycine. Acta Cryst 11:17–31.CrossRefGoogle Scholar
  145. Low BW, Baybutt RB (1952) The π-helix — A hydrogen bonded configuration of the polypeptide chain. J Am Chem Soc 74:5806–5807.CrossRefGoogle Scholar
  146. Low BW, Grenville-Wells (1953) Generalized mathematical relationships for polypeptide chain helices. The coordinates of the π-helix. Proc Natl Acad Sci USA 39:785–801.PubMedCrossRefGoogle Scholar
  147. Main P (1967) Phase determination using non-crystallo-graphic symmetry. Acta Cryst 23:50–54.CrossRefGoogle Scholar
  148. Main P, Rossmann MG (1966) Relationships among structure factors due to identical molecules in different crystallographic environments. Acta Cryst 21:67–72.CrossRefGoogle Scholar
  149. Mark H, Szilard L (1925) Ein einfacher Versuch zur Auffindung eines selektiven Effektes bei der Zerstreuung von Röntgenstrahlen. Z Phys 33:688–691.CrossRefGoogle Scholar
  150. Matthews BW (1966a) The extension of the isomorphous replacement method to include anomalous scattering measurements. Acta Cryst 20:82–86.CrossRefGoogle Scholar
  151. Matthews BW (1966b) The determination of the position of anomaiously scattering heavy atom groups in protein crystals. Acta Cryst 20:230–239.CrossRefGoogle Scholar
  152. Matthews BW, Colman PM, Jansonius JN, Titani K, Walsh KA, Neurath H (1972b) Structure of thermolysin. Nature New Biol 238:41–43.PubMedCrossRefGoogle Scholar
  153. Matthews BW, Jansonius JN, Colman PM, Schoenborn BP, Dupourque D (1972a) Three-dimensional structure of thermolysin. Nature New Biol 238:37–41.PubMedCrossRefGoogle Scholar
  154. Matthews BW, Sigler PB, Henderson R, Blow DM (1967) Three-dimensional structure of tosyl-α-chymotrpysin. Nature 214:652–656.PubMedCrossRefGoogle Scholar
  155. Meselson M, Stahl FW (1958) The replication of DNA in Escherichia Coli. Proc Natl Acad Sci USA 44:671–682.PubMedCrossRefGoogle Scholar
  156. Meyer KH, Mark H (1928a) Über den Bau des krystallisierten Anteils der Cellulose. Ber Dtsch Chem Ges 61:593–614.CrossRefGoogle Scholar
  157. Meyer KH, Mark H (1928b) Über den Aufbau des Seiden-Fibroins. Ber Dtsch Chem Ges 61:1932–1936.CrossRefGoogle Scholar
  158. Meyer KH, Mark H (1928c) Über den Aufbau des Chitins. Ber Dtsch Chem Ges 61:1936–1939.CrossRefGoogle Scholar
  159. Meyer KH, Mark H (1928d) Über den Kautschuk. Ber Dtsch Chem Ges 61:1939–1949.CrossRefGoogle Scholar
  160. Michel H (1982) Three-dimensional crystals of a membrane protein complex. The photosynthetic reaction center from Rhodopseudomonas viridis. J Mol Biol 158:562–567.CrossRefGoogle Scholar
  161. Mitscherlich E (1819) Über die Kristallisation der Salze in denen das Metall der Basis mit zwei Proportionen Sauerstoff verbunden ist. Abh Kgl Akad Wiss (Berlin): 427-437.Google Scholar
  162. Monod J, Wyman J, Changeux J-P (1965) On the nature of allosteric transitions: A plausible model. J Mol Biol 12:88–118.PubMedCrossRefGoogle Scholar
  163. Muirhead H, Greer J (1970) Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 3, 5 Å resolution. Nature 228:516–519.PubMedCrossRefGoogle Scholar
  164. Muirhead H, Cox JM, Mazzarella L, Perutz MF (1967) Structure and function of haemoglobin. III. A threedimensional Fourier synthesis of human deoxyhaemogiobin at 5,5 Å resolution. J Mol Biol 28:117–156.PubMedCrossRefGoogle Scholar
  165. Nishikawa S, Ono S (1913) Transmission of X-rays through fibrous, lamellar and granular substances. Proc Tokyo Math Phys Soc 7:131–138.Google Scholar
  166. Nishikawa S, Matukawa K (1928) Hemihedry of zinc blende and X-ray reflection. Proc Imp Acad (Japan) 4:96–97.Google Scholar
  167. Nordman CE, Nakatsu K (1963) Interpretation of the Patterson function of crystals containing a known molecular fragment. The structure of an alstonine alkaloid. J Am Chem Soc 85:353–354.CrossRefGoogle Scholar
  168. North ACT (1965) The combination of isomorphous replacement and anomalous scattering data in phase determination of non-centrosymmetric reflexions. Acta Cryst 18:212–216.CrossRefGoogle Scholar
  169. Patterson AL (1934) A Fourier series method for the determination of the components of interatmic distances in crystals, Phys Rev 46:372–376.CrossRefGoogle Scholar
  170. Patterson AL (1935) A direct method for the determination of the components of interatomic distances in crystals. Z Krist A90:517–542.Google Scholar
  171. Pauling L, Sherman J (1933) The nature of the chemical bond. VI. The calculation from thermochemical data of the energy of resonance of molecules among several electronic structures. J Chem Phys 1:606–617.CrossRefGoogle Scholar
  172. Pauling L, Corey RB (1950) Two hydrogen-bonded spiral configurations of the poiypeptide chain. J Am Chem Soc 72:5349.CrossRefGoogle Scholar
  173. Pauling L, Corey RB (1951a) Atomic coordinates and structure factors for two helical configurations of poiypeptide chains. Proc Natl 37:235–240.CrossRefGoogle Scholar
  174. Pauling L, Corey RB (1951b) The pleated sheet, a new layer configuration of poiypeptide chains. Proc Natl Acad Sci USA 37:251–256.PubMedCrossRefGoogle Scholar
  175. Pauling L, Corey RB (1951c) The structure of hair, muscle and related proteins. Proc Natl Acad Sci USA 37:261–271.PubMedCrossRefGoogle Scholar
  176. Pauling L, Corey RB (1951d) The structure of fibrous proteins of the collagen-gelatin group. Proc Natl Acad Sci USA 37:272–281.PubMedCrossRefGoogle Scholar
  177. Pauling L, Corey RB (1953) Compound helical configurations of poiypeptide chains: Structure of proteins of the a-keratin type. Nature 171:59–61.PubMedCrossRefGoogle Scholar
  178. Pauling L, Corey RB, Branson HR (1951)The structure of proteins: Two hydrogen-bonded helical configurations of the poiypeptide chain. Proc Natl Acad Sci USA 37:205–211.PubMedCrossRefGoogle Scholar
  179. Perutz MF (1949) X-ray studies of crystalline proteins. Research 2:52–61.PubMedGoogle Scholar
  180. Perutz MF (1951) New X-ray evidence on the configuration of poiypeptide chains. Poiypeptide chains m poly-γ-benzyi.L-glutamate, keratin and haemoglobin. Nature 167:1053–1054.PubMedCrossRefGoogle Scholar
  181. Perutz MF (1956) Isomorphous replacement and phase determination in non-centrosymmetric space groups. Acta Cryst 9:867–873.CrossRefGoogle Scholar
  182. Perutz MF (1970) Stereochemistry of cooperative effects in haemoglobin. Nature 228:726–734.PubMedCrossRefGoogle Scholar
  183. Perutz MF (1971) Geleitwort. In: Dickerson RE, Geis I (Hrsg) Struktur und Funktion der Proteine. Verlag Chemie, Weinheim.Google Scholar
  184. Perutz MF, Muirhead H, Cox JM, Goaman LCG, Mathews FS, McGandy EL, Webb LE (1968a) Threedimensional Fourier synthesis of horse oxyhaemoglobin at 2,8 Å resolution. I. X-ray analysis. Nature 219:29–32.PubMedCrossRefGoogle Scholar
  185. Perutz MF, Muirhead H, Cox JM, Goaman LCG (1968b) Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2,8 A resolution. II The atomic model. Nature 219:131–139.PubMedCrossRefGoogle Scholar
  186. Pflugrath W (1992) Developments in X-ray detectors. Curr Opin Struct Biol 2:811–815.CrossRefGoogle Scholar
  187. Polanyin M (1921) Faserstruktur im Röntgenlichte. Naturwissenschaften 9:337–340.CrossRefGoogle Scholar
  188. Prins JA (1928) Über die Dispersion und Absorption von Röntgenstrahlen. Z Phys 47:479–498.CrossRefGoogle Scholar
  189. Ramachandran GN, Kartha G (1954) Structure of collagen. Nature 174:269–270.PubMedCrossRefGoogle Scholar
  190. Ramachandran GN, Kartha G (1955) Structure of collagen. Nature 176:593–595.PubMedCrossRefGoogle Scholar
  191. Ramachandran GN, Raman S (1956) New method for the structure analysis of noncentrosy m metric crystals. Curr Sci 25:348–351.Google Scholar
  192. Rich A, Crick FHC (1955) The structure of collagen. Nature 176:915–916.PubMedCrossRefGoogle Scholar
  193. Richards FM (1968) The matching of physical models to three-dimensional electron-density maps: A simple optical device. J Mol Biol 37:225–230.PubMedCrossRefGoogle Scholar
  194. Riggs AF (1952) Sulfhydryi groups and the interaction between the hems in hemoglobin. J Gen Physiol 36:1–16.PubMedCrossRefGoogle Scholar
  195. Robertson JM (1936) An X-ray study of phthalocyanines. Part II Quantitative structure determination of the metal-free compound. J Chem Soc 1195-1209.Google Scholar
  196. Robertson JM (1939) Vector maps and heavy atoms in crystal analysis and the insulin structure. Nature 143:75–76.CrossRefGoogle Scholar
  197. Rossmann MG (1960) The accurate determination of the position and shape of heavy-atom replacement groups in Proteins. Acta Cryst 13:221–226.CrossRefGoogle Scholar
  198. Rossmann MG (1961) The position of anomalous scatterers in protein crystals. Acta Cryst 14:383–388.CrossRefGoogle Scholar
  199. Rossmann MG, Blow DM (1962) The detection of subunits within the crystallographic asymmetric unit. Acta Cryst 15:24–31.CrossRefGoogle Scholar
  200. Rossmann MG, Blow DM (1963) Determination of phases by the conditions of non-crystallographic symmetry, Acta Cryst 16:39–45.CrossRefGoogle Scholar
  201. Rühlmann A, Kukla D, Schwager P, Bartels K, Huber R (1973) Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. I. Crystal structure determination and stereochemistry of the contact region. J Moi Biol 77:417–436.CrossRefGoogle Scholar
  202. Sayre D (1974) Least-squares phase refinement. II. Highresolution Phasing of a small protein. Acta Cryst A30:180–184.Google Scholar
  203. Schulz GE, Schirmer RH (1978) Principles of protein structure. Springer, New York.Google Scholar
  204. Segal DM, Cohen GC, Davies DR, Powers JC, Wilcox PE (1971a) The stereochemistry of substrate binding to chymotrypsin Ay. Cold Spring Harbour Symp Quant Biol 36:85–90.CrossRefGoogle Scholar
  205. Segal DM, Powers JC, Cohen GC, Davies DR, Wilcox PE (1971b) Substrate binding sites in bovine chymotrypsin Aγ. A crystallographic study using peptide chloromethyl ketones as site-specific inhibitors. Biochemistry 10:3728–3738.PubMedCrossRefGoogle Scholar
  206. Shotton DM, Watson HC (1970) Three-dimensional structure of tosyl-elastase. Nature 225:811–816.PubMedCrossRefGoogle Scholar
  207. Staudinger H (1926) Die Chemie der hochmolekularen orgnischen Stoffe im Sinne der Kekuléschen Strukturlehre. Ber Dtsch Chem Ges 59:3019–3043.CrossRefGoogle Scholar
  208. Steinbacher S, Seckler R, Miller S, Steipe B, Huber R, Reinemer P (1994) X-ray structure of a shortened P22 tailspike: Intcrdigitated subunits in a thermostabie trimer. Science 265:383–386.PubMedCrossRefGoogle Scholar
  209. Steitz TA, Henderson R, Blow DM (1969) Structure of crystalline α-chymotrypsin. III, Crystallographic studies of substrates and inhibitors bound to the active site of α-chymotrypsin. J Moi Biol 46:337–348.CrossRefGoogle Scholar
  210. Stokes AR (1955) The theory of X-ray fibre diagramms. Prog Biophys 5:140–167.Google Scholar
  211. Stroud RM, Kay LM, Dickerson RE (1971) The crystal and molecular structure of DIP-inhibited bovine trypsin at 2,7 Å resolution. Cold Spring Harbour Symp Quant Biol 36:125–140.CrossRefGoogle Scholar
  212. Stuart DI, Jones EY (1993) Weissenberg data collection for macromolecular crystallography. Curr Opin Struct Biol 3:737–740.CrossRefGoogle Scholar
  213. Sussman JL, Holbrook SR, Church GM, Kim SH (1977) A structure-factor least-squares refinement procedure for macromoiecular structures using constrained and restrained parameters. Acta Cryst A 33:800–804.CrossRefGoogle Scholar
  214. Sweet RM, Wright HT, Janin J, Chothia CH, Clow DM (1974) Crystal structure of the complex of bovine trypsin with soybean trypsin inhibitor (Kunitz) at 2,6Å resolution. Biochemistry 13:4212–4228.PubMedCrossRefGoogle Scholar
  215. Tollin P (1966) On the determination of molecular location. Acta Cryst 21:613–614.CrossRefGoogle Scholar
  216. Tollin P (1969) Determination of the orientation and position of the myoglobin molecule in the crystal of seal myoglobin. J Mol Biol 45:481–490.PubMedCrossRefGoogle Scholar
  217. Tollin P, Rossmann MG (1966) A description of various rotation function programms. Acta Cryst 21:872–876.CrossRefGoogle Scholar
  218. Warren B, Bragg WL (1928) The structure of diopoide, CaMg(SiO3)2. Z Krist 69:168–193.Google Scholar
  219. Warren BE, Gingrich NS (1934) Fourier integral analysis of X-ray powder patterns. Phys Rev 46:368–372.CrossRefGoogle Scholar
  220. Waser J (1963) Least-squares refinement with subsidiary conditions, Acta Cryst 16:1091–1094.CrossRefGoogle Scholar
  221. Watenpaugh KD, Sieker LC, Herriot JR, Jensen LH (1973) Refinement of the model of a protein: Rubredoxin at 1,5 Å resolution. Acta Cryst B29:943–956.Google Scholar
  222. Watson HC, Shotton DM, Cox JM, Muirhead H (1970) Three-dimensional Fourier synthesis of Tosyl-elastase at 3,5 Å resolution. Nature 225:806–811.PubMedCrossRefGoogle Scholar
  223. Watson JD, Crick FHC (1953a) A structure of deoxyribose nucleic acid. Nature 171:737–738.PubMedCrossRefGoogle Scholar
  224. Watson JD, Crick FHC (1953b) Geneticai implications of the sturcture of deoxyribonucleic acid. Nature 171:962–967.CrossRefGoogle Scholar
  225. Weiss MS, Wacker T, Weckesser J, Weite W, Schultz GE (1990) The three-dimensional structure of porin from rhodobacter capsulatus at 3 Å resolution. FEBS Lett 267:268–272.PubMedCrossRefGoogle Scholar
  226. Weissenberg K (1924) Ein neues Röntgengoniometer. ZPhys 23:229–238.Google Scholar
  227. Wilkins MHF, Randall JT (1953) Crystalllnity in sperm heads: Molecular structure of nucleoprotein in vivo. Biochim Biophys Acta 10:192–193.PubMedCrossRefGoogle Scholar
  228. Wilkins MHF, Gosling RG, Seeds WE (1951) Nucleic acid: An extensible molecule. Nature 167:759–760.PubMedCrossRefGoogle Scholar
  229. Wilkins MHF, Stokes AR, Wilson HR (1953a) Molecular structure of deoxypenstose nucleic acids. Nature 171:738–740.PubMedCrossRefGoogle Scholar
  230. Wilkins MHF, Seeds WE, Stokes AR, Wilson HR (1953b) Helical structure of crystalline deoxypentose nucleic acid. Nature 172:759–762.PubMedCrossRefGoogle Scholar
  231. Wright CS, Alden RA, Kraut J (1969) Structure of subtilisin BPN’ at 2,5 Å resolution. Nature 221:235–242.PubMedCrossRefGoogle Scholar
  232. Wütherich K (1989) Protein structure determination in solution by nuclear magnetic resonance spectroscopy. Science 243:45–50.CrossRefGoogle Scholar
  233. Wyckoff HW, Hardman KD, Alleweil NM, Inagami T, Tsernoglou D, Johnson LN, Richards FM (1967a) The structure of ribonuclease-S at 6 Å resolution. J Biol Chem 242:3749–3753.PubMedGoogle Scholar
  234. Wyckoff HW, Hardman KD, Alleweil NM, Inagami T, Johnson LN, Richards FM (1967b) The structure of ribonuciease-S at 3,5 Å resolution. J Biol Chem 242:3984–3988.PubMedGoogle Scholar
  235. Wyckoff RWG, Corey RB (1936) X-ray diffraction patterns of crystalline tobacco mosaic virus. J Biol Chem 116:51–56.Google Scholar
  236. Yakel HL jr, Hughes EW (1954) The crystal structure of N,N’-diglycyl-L-cysteine Dihydrate. Acta Cryst 7:291–297.CrossRefGoogle Scholar
  237. Yoder MD, Keen NT, Jurnak F (1993) New domain motif: The structure of pectate lyase C, a secreted plant virulence factor. Science 260:1503–1507.PubMedCrossRefGoogle Scholar
  238. Zernike F, Prins JA (1927) The bending of X-rays in liquid as an effect of molecular arrangement. Z Phys 41:184–194.CrossRefGoogle Scholar

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© Springer-Verlag Berlin Heidelberg 1995

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  • Peter Reinemer
  • Robert Huber

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