Abstract
Hemoglobin (Hb) crystallization is of significance both in vivo and in vitro. Hb crystals form in red blood cells (RBCs), as occurs in the case of patients expressing βC-globin (β6 Glu→Lys). In vitro, high-resolution structural determination by crystallographic methods requires the growth of Hb crystals to approx ∼1 mm in diameter, which may be induced by a variety of precipitants.
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References
Haurowitz, F. (1938) Das Gleichgewicht zwischen Hamoglobin und Sauerstoff. Z. Physiol. Chem. 254, 266–274.
Perutz, M. F. and Mathews, F. S. (1966) An x-ray study of azide methaemoglobin. J. Mol. Biol. 21(1), 199–202.
Perutz, M. F. and Lehmann, H. (1968) Molecular pathology of human haemoglobin. Nature 219(157), 902–909.
Perutz, M. F. (1969) The Croonian Lecture, 1968. The haemoglobin molecule. Proc. R. Soc. Lond. B. Biol. Sci. 173(31), 113–140.
Nagel, R. L. (1991) The distinct pathobiology of SC disease: therapeutic tmplications, in Hematology/Oncology Clinics of North America, vol. (Nagel, R. L., ed.), W. B. Saunders, Philadelphia, pp. 433–451.
Nagel, R. L. and Steinberg, M. H. (2000) Hb SC and Hb C disease, in Disorders of Hemoglobin: Genetics, Pathophysiology, Clinical Management, (Steinberg, M. H., Forget, B. G., Higgs, D. R., Nagel, R. L., eds.), Cambridge University Press, MA.
Diggs, L. W. and Kraus, A. P. (1954) Intraerythrocytic crystals in a white patient with hemoglobin C in the absence of other types of hemoglobin. Blood 9, 1172–1184.
Kraus, A. P. and Diggs, L. W. (1956) In vitro crystallization of hemoglobin occurring in citrated blood from patients with hemoglobin. C. J. Lab. Clin. Med. 47, 700–705.
Charache, S., Conley, C. L., Waugh, D. F., Ugoretz, R. J., and Spurrell, J. R. (1967) Pathogenesis of hemolytic anemia in homozygous hemoglobin C disease. J. Clin. Invest. 46(11), 1795–811.
Hirsch, R. E., Raventos-Suarez, C., Olson, J. A., and Nagel, R. L. (1985) Ligand state of intraerythrocytic circulating HbC crystals in homozygote CC patients. Blood 66(4), 775–777.
Bunn, H. F., Noguchi, C. T., Hofrichter, J., Schechter, G. P., Schechter, A. N., and Eaton, W. A. (1982) Molecular and cellular pathogenesis of hemoglobin SC disease. Proc. Natl. Acad. Sci. USA 79(23), 7527–7531.
Lawrence, C., Fabry, M. E., and Nagel, R. L. (1991) The unique red cell heterogeneity of SC disease: crystal formation, dense reticulocytes, and unusual morphology. Blood 78(8), 2104–2112.
Hirsch, R. E., Lin, M. J., and Nagel, R. L. (1988) The inhibition of hemoglobin C crystallization by hemoglobin F. J. Biol. Chem. 263(12), 5936–5939.
Adachi, K. and Asakura, T. (1981) Aggregation and crystallization of hemoglobins, A., S, and, C., Probable formation of different nuclei for gelation and crystallization. J. Biol. Chem. 256(4), 1824–1830.
Adachi, K., Segal, R., and Asakura, T. (1980) Nucleation controlled agregation of deoxyhemoglobin. S. J. Biol. Chem. 255, 7595–7603.
Kashchiev, D. (1969) Solution of the non-steady state problem in nucleation kinetics. Surf. Sci. 14, 209–220.
Kashchiev, D., (1995) Nucleation, in Science and Technology of Crystal Growth (van Eerden J. P. and Bruinsma, O. S. L., eds.), Kluwer Academic, Norwell, MA, pp. 53–56.
Mutaftschiev, B. (1993) Nucleation theory, in Handbook of Crystal Growth, vol. 1 (Hurle, D. T. J., ed.), Elsevier, Amsterdam, pp. 189–247.
Weber, P. (1991) Physical principles of protein crystallization, in Advances in Protein Chemistry, vol. 41 (Afinsen, C. B., Richards, F. M., Edsal, J. T., and Eisenberg, D. S., eds.), Academic, New York.
Weber, P. C. (1997) Overview of protein crystallization methods, in Methods in Enzymology, vol. 276. (Carter, C. W. Jr. and Sweet, R. M., eds.), Academic, New York, pp. 13–22.
Lin, M. J., Nagel, R. L., and Hirsch, R. E. (1989) The acceleration of hemoglobin C crystallization by hemoglobin S. Blood 74, 1823–1825.
Nagel, R. L., Lin, M. J., Witkowska, H. E., Fabry, M. E., Bestak, M., and Hirsch, R. E. (1993) Compound heterozygosity for hemoglobin C and Korle-Bu: moderate microcytic hemolytic anemia and acceleration of crystal formation [corrected] [published erratum appears in Blood 1994; 83(10):3105]. Blood 82(6), 1907–1912.
Hirsch, R. E., Witkowska, H. E., Shafer, F., Lin, M. J., Balazs, T. C., Bookchin, R. M., and Nagel, R. L. (1997) HbC compound heterozygotes [HbC/Hb Riyadh and HbC/Hb N-Baltimore] with opposing effects upon HbC crystallization. Br. J. Haematol. 97(2), 259–265.
Lawrence, C., Hirsch, R. E., Fataliev, N. A., Patel, S., Fabry, M. E., and Nagel, R. L. (1997) Molecular interactions between Hb alpha-G Philadelphia, HbC, and HbS: phenotypic implications for SC alpha-G Philadelphia disease. Blood 90(7), 2819–2825.
Hirsch, R. E., Shafer, F., Wajcman, H., Fataliev, N., and Nagel, R. L. (1999) HbJ-Baltimore Favors Crystallization of OxyHbC, but chain assembly abnormalities blunt the phenotype of the compound heterozygote. Blood 92(10)(Suppl. 1, Pt. 1), 11a.
Adachi, K., Lai, C. H., Konitizer, P., Donahee, M., and Campbell, A., S. S. (1994) Crystallization of recombinant hemoglobins with basic amino acid substitutions (Lys and Arg) at the 6 position. Blood 84, 1309–1313.
Gallagher, D. T., Eisenstein, E., Fisher, K. E., et al. (1998) Polymorphous crystallization and diffraction of threonine deaminase from Escherichia coli. Acta. Cryst. D. 54, 467–469.
Hirsch, R. E., Samuel, R. E., Fataliev, N. A., Pollack, M. J., Galkin, O., Vekilov, P. G., and Nagel, R. L. (2001) Differential pathways in oxy and deoxy HbC aggregation/crystallization [in process citation]. Proteins 42(1), 99–107.
Feeling-Taylor, A. R., Banish, R. M., Hirsch, R. E., and Vekilov, P. G. (1999) Miniaturized scinitillation technique for protein solubility determinations. Rev. Sci. Instr. 70(6), 2845–2849.
Cabrera, N. and Vermileya, D. A. (1958) The growth of crystals form solution, in Growth and Perfection of Crystals (Doremus, R. H., Roberts, B. W., and Turnbul, D., eds.), Wiley, New York.
Voronkov, V. V. and Rashkovich, L. N. (1994) Step kinetics in the presence of mobile adsorbed impurity. J. Crystal Growth 144, 107–115.
Dewan, J. C., Feeling-Taylor, A., Puius, Y. A., et al. (2002) Structure of mutant human carbonmonoxyhemoglobin C (βE6K) at 2.0 Å resolution. Acta. Crystallogr. D58, 2038–2042.
Rosenberger, F., Howard, S. B., Sowers, J. W., and Nyce, T. A. (1993) Temperature dependence of protein solubility—determination and application to crystallization in X-ray capillaries. J. Crystal Growth 129, 1–12.
Hansma, H. G. and Hoh, J. H. (1994) Biomolecular imaging with the atomic force microscope. Annu. Rev. Biophys. Biomol. Struct. 23, 115–139.
Hansma, P. K., Cleveland, J. P., Radmacher, M., et al. (1994) Tapping mode atomic force microscopy in liquids. Appl. Phys. Lett. 64(13), 1738–1740.
Möller, C., Allen, M., Elings, V., Engel, A., and Müller, D. J. (1999) Tapping-mode atomic microscopy produces faithful high-resolution images of protein surfaces. Biophys. J. 77, 1150–1158.
Noy, A., Sanders, C. H., Vezenov, D. V., Wong, S. S., and Lieber, C. M. (1998) Chemically sensitive imaging in tapping mode by chemical force microscopy: relationship between phase lag and adhesion. Langmuir 14, 1508–1511.
Yau, S.-T., Petsev, D. N., Thomas, B. R., and Vekilov, P. G. (2000) Molecular-level thermodynamic and kinetic parameters for the self-assembly of apoferritin molecules into crystals. J. Mol. Biol. 303(5), 667–678.
Fitzgerald, P. M. and Love, W. E. (1979) Structure of deoxy hemoglobin C (beta six Glu replaced by Lys) in two crystal forms. J. Mol. Biol. 132(4), 603–619.
Volmer, M. (1939) Kinetik der Phasenbildung. Steinkopff, Dresden.
Giesen, M., Schulze Icking-Konert, G., Stapel, D., and Ibach, H. (1996) Step fluctuations on Pt(111) surfaces. Surface Sci. 366, 229–238.
Malkin, A. J., Kuznetsov, Y. G., Land, T. A., DeYoreo, J. J., and McPherson, A. (1996) Mechanisms of growth of protein and virus crystals. Nat. Struct. Biol. 2, 956–959.
McPherson, A., Malkin, A. J., and Kuznetsov, Y. G. (2000) Atomic force microscopy in the study of macroimoleular crystal growth. Annu. Rev. Biomol. Struct. 20, 361–410.
Yip, C. M. and Ward, M. D. (1996) Atomic force microscopy of insulin single crystals: direct visulization of molecules and crystal growth. Biophysical J. 71, 1071–1078.
Thomas, B. R., Vekilov, P. G., and Rosenberger, F. (1998) Effects of microhetero-geneity on hen egg white lysozyme crystallization. Acta Crystallogr. Sect. D 54, 226–236.
Thomas, B. R., Vekilov, P. G., and Rosenberger, F. (1996) Heterogeneity determination and purification of commercial hen egg white lysozyme. Acta Crystallogr. Sect. D 52, 776–784.
Vekilov, P. G. (1993) Elementary processes of protein crystal growth, in Studies and Concepts in Crystal Growth (Komatsu, H., ed.), Pergamon, Oxford: pp. 25–49.
Vekilov, P. G., Monaco, L. A., and Rosenberger, F. (1995) Facet morphology response to non-uniformities in nutrient and impurity supply. I. Experiments and interpretation. J. Crystal Growth 156, 267–278.
Vekilov, P. G. and Rosenberger, F. (1996) Dependence of lysozyme growth kinetics on step sources and impurities. J. Crystal Growth 158, 540–551.
Stojanoff, V., Siddons, D. P., Monaco, L. A., Vekilov, P. G., and Rosenberger, F. (1997) X-ray topography of tetragonal lysozyme grown by the temperature controlled technique. Acta Crystallogr. Sect. D 53, 588–595.
Vekilov, P. G., Monaco, L. A., Thomas, B. R., Stojanoff, V., and Rosenberger, F. (1996) Repartitioning of NaCl and protein impurities in lysozyme crystallization. Acta Crystallogr. Sect. D 52, 785–798.
Hirsch, R. E., Rybicki, A. C., Fataliev, N. A., Lin, M. J., Friedman, J. M., and Nagel, R. L. (1997) A potential determinant of enhanced crystallization of Hbc: spectroscopic and functional evidence of an alteration in the central cavity of oxyHbC. Br. J. Haematol. 98(3), 583–588.
Monaco, L. A. and Rosenberger, F. (1993) Growth and etching kinetics of tetragonal lysozyme. J. Crystal Growth 129, 465–484.
Samuel, R. E., Salmon, E. D., and Briehl, R. W. (1990) Nucleation and growth of fibres and gel formation in sickle cell haemoglobin. Nature 345, 833–835.
Schroeder, W. A. and Huisman, T. H. J. (1980) The Chromatography of Hemoglobin, Marcel Dekker, New York.
Adachi, K. and Asakura, T. (1979) Gelation of deoxyhemoglobin A in concentrated phosphate buffer. Exhibition of delay time prior to aggregation and crystallization of deoxyhemoglobin, A., J. Biol. Chem. 254(24), 12,273–12,276.
Adachi, K. and Asakura, T. (1979) Nucleation-controlled aggregation of deoxyhemoglobin S: possible difference in the size of nuclei in different phosphate concentrations. J. Biol. Chem. 254(16), 7765–7771.
Adachi, K. and Asakura, T. (1979) The solubility of sickle and non-sickle hemoglobins in concentrated phosphate buffer. J. Biol. Chem. 254(10), 4079–4084.
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Vekilov, P.G., Feeling-Taylor, A., Hirsch, R.E. (2003). Nucleation and Crystal Growth of Hemoglobins. In: Nagel, R.L. (eds) Hemoglobin Disorders. Methods in Molecular Biology™, vol 82. Humana Press. https://doi.org/10.1385/1-59259-373-9:155
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DOI: https://doi.org/10.1385/1-59259-373-9:155
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