Abstract
Already early protein crystallization experiments in space indicated that more extended crystallization periods, beyond the flight durations of shuttle missions or unmanned orbiters, will be beneficial for the majority of microgravity protein crystal growth experiments. Beside preceding intensive efforts to adjust and optimize crystallization conditions to meet the microgravity time span of orbiters flight duration, video imaging of some experiments showed that the crystallization process was not finalized at the end of the mission. And a number of experiments performed on MIR, prior to availability of ISS, confirmed potential advantages applying extended microgravity crystallization periods, also knowing that due to some crew activities the microgravity on ISS may not sustain a 100% convection free environment in the crystallization hardware. Considering this fact as a minor restraint and knowing that most biomolecules require and appreciate growth periods longer than the duration of a typical shuttle mission of 7–10 days, opportunities to perform crystallization experiments on ISS are very attractive.
References
Akparov VK, Timofeev VI, Kuranova IP (2015) Crystallization and preliminary X-ray diffraction study of porcine carboxypeptidase B. Crystallogr Rep 60(3):367–369. doi:10.1134/s1063774515030025
Barnes CL, Snell EH, Kundrot CE (2002) Thaumatin crystallization aboard the International Space Station using liquid–liquid diffusion in the Enhanced Gaseous Nitrogen Dewar (EGN). Acta Crystallogr D Biol Crystallogr 58(5):751–760
Berisio R, Vitagliano L, Vergara A, Sorrentino G, Mazzarella L, Zagari A (2002) Crystallization of the collagen-like polypeptide (PPG) 10 aboard the International Space Station. 2. Comparison of crystal quality by X-ray diffraction. Acta Crystallogr D Biol Crystallogr 58(10):1695–1699
Bosch R, Lautenschlager P, Potthast L, Stapelmann J (1992) Experiment equipment for protein crystallization in μg facilities. J Cryst Growth 122(1–4):310–316
Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A (2001) Video observation of protein crystal growth in the advanced protein crystallization facility aboard the space shuttle mission STS-95. J Cryst Growth 232(1–4):481–488. doi:10.1016/S0022-0248(01)01084-3
DeLucas LJ, Crysel WB, Weise LD, Smith CD, McDonald WT (1999) The international space station X-ray crystallography facility. Adv X-ray Anal 43:1999
DeLucas LJ, Long MM, Moore KM, Harrington M, McDonald WT, Smith CD, Lewis TB, Crysel WB, Weise LD (2000) Protein crystal growth studies at the center for macromolecular crystallography. Space Technology and Application Forum, pp 488–490
Edward HS, John RH (2005) Macromolecular crystallization in microgravity. Rep Prog Phys 68(4):799
Evrard C, Maes D, Zegers I, Declercq J-P, Vanhee C, Martial J, Wyns L, Weerdt CVD (2007) TIM crystals grown by capillary counterdiffusion: statistical evidence of quality improvement in microgravity. Cryst Growth Des 7(11):2161–2166. doi:10.1021/cg700687t
Gonzalez-Ramirez LA, Carrera J, Gavira JA, Melero-Garcia E, Garcia-Ruiz JM (2008) Granada crystallization facility-2: a versatile platform for crystallization in space. Cryst Growth Des 8(12):4324–4329
Habash J, Boggon TJ, Raftery J, Chayen NE, Zagalsky PF, Helliwell JR (2003) Apocrustacyanin C(1) crystals grown in space and on Earth using vapour-diffusion geometry: protein structure refinements and electron-density map comparisons. Acta Crystallogr D Biol Crystallogr 59(Pt 7):1117–1123
Inaka K, Takahashi S, Aritake K, Tsurumura T, Furubayashi N, Yan B, Hirota E, Sano S, Sato M, Kobayashi T, Yoshimura Y, Tanaka H, Urade Y (2011) High-quality protein crystal growth of mouse lipocalin-type prostaglandin D synthase in microgravity. Cryst Growth Des 11(6):2107–2111. doi:10.1021/cg101370v
Kinoshita T, Maruki R, Warizaya M, Nakajima H, Nishimura S (2005) Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method. Acta Crystallogr Sect F: Struct Biol Cryst Commun 61(4):346–349
Krauspenhaar R, Rypniewski W, Kalkura N, Moore K, DeLucas L, Stoeva S, Mikhailov A, Voelter W, Betzel C (2002) Crystallisation under microgravity of mistletoe lectin I from Viscum album with adenine monophosphate and the crystal structure at 1.9 A resolution. Acta Crystallogr D Biol Crystallogr 58(pt 10 pt 1):1704–1707
Kuranova I, Smirnova E, Abramchik YA, Chupova L, Esipov R, Akparov VK, Timofeev V, Kovalchuk M (2011) Crystal growth of phosphopantetheine adenylyltransferase, carboxypeptidase t, and thymidine phosphorylase on the international space station by the capillary counter-diffusion method. Crystallogr Rep 56(5):884
Małecki PH, Rypniewski W, Szymański M, Barciszewski J, Meyer A (2012) Binding of the plant hormone kinetin in the active site of Mistletoe Lectin I from Viscum album. Biochim Biophys Acta 1824(2):334–338
McPherson A (2004) Introduction to protein crystallization. Methods 34(3):254–265
McPherson A, Malkin AJ, Kuznetsov YG, Koszelak S, Wells M, Jenkins G, Howard J, Lawson G (1999) The effects of microgravity on protein crystallization: evidence for concentration gradients around growing crystals. J Cryst Growth 196(2):572–586
Meyer A, Rypniewski W, Szymański M, Voelter W, Barciszewski J, Betzel C (2008) Structure of mistletoe lectin I from Viscum album in complex with the phytohormone zeatin. Biochim Biophys Acta 1784(11):1590–1595
Miele AE, Federici L, Sciara G, Draghi F, Brunori M, Vallone B (2003) Analysis of the effect of microgravity on protein crystal quality: the case of a myoglobin triple mutant. Acta Crystallogr D Biol Crystallogr 59(pt 6):982–988
Mohamad Aris SNA, Thean Chor AL, Mohamad Ali MS, Basri M, Salleh AB, Raja Abd Rahman RNZ (2014) Crystallographic analysis of ground and space thermostable T1 lipase crystal obtained via counter diffusion method approach. Biomed Res Int 2014:8. doi:10.1155/2014/904381
Nichesola D, Perduca M, Capaldi S, Carrizo ME, Righetti PG, Monaco HL (2004) Crystal structure of chicken liver basic fatty acid-binding protein complexed with cholic acid. Biochemistry 43(44):14072–14079
Pletser V, Stapelmann J, Potthast L, Bosch R (1999) The Protein Crystallization Diagnostics Facility, a new European instrument to investigate biological macromolecular crystal growth on board the International Space Station. J Cryst Growth 196(2):638–648
Pletser V, Bosch R, Potthast L, Kassel R (2006) The Solution Crystallisation Diagnostics Facility, a European Facility for Microgravity Research on Structures from Solutions on Board the ISS. Fluid Dyn Mater Process 2(1):65–76
Pletser V, Bosch R, Potthast L, Lautenschlager P, Kassel R (2009) The Protein Crystallisation Diagnostics Facility (PCDF) on Board ESA Columbus Laboratory. Microgravity Sci Technol 21(3):269–277
Ponassi M, Felli L, Parodi S, Valbusa U, Rosano C (2011) Crystals of the hydrogenase maturation factor HypF N-terminal domain grown in microgravity, display improved internal order. J Crys Growth 314(1):246–251. doi:10.1016/j.jcrysgro.2010.12.011
Safonova TN, Mordkovich NN, Polyakov KM, Manuvera VA, Veiko VP, Popov VO (2012) Crystallization of uridine phosphorylase from Shewanella oneidensis MR-1 in the laboratory and under microgravity and preliminary X-ray diffraction analysis. Acta Crystallogr Sect F: Struct Biol Cryst Commun 68(pt 11):1387–1389. doi:10.1107/S1744309112041784
Sato M, Tanaka H, Inaka K, Shinozaki S, Yamanaka A, Takahashi S, Yamanaka M, Hirota E, Sugiyama S, Kato M (2006) JAXA-GCF project-high-quality protein crystals grown under microgravity environment for better understanding of protein structure. Microgravity Sci Technol 18(3):184–189
Shabalin IG, Serov AE, Skirgello OE, Timofeev VI, Samygina VR, Popov VO, Tishkov VI, Kuranova IP (2010) Recombinant formate dehydrogenase from Arabidopsis thaliana: Preparation, crystal growth in microgravity, and preliminary X-ray diffraction study. Crystallogr Rep 55(5):806–810. doi:10.1134/s1063774510050159
Simic-Stefani S, Kawaji M, Hu HH (2006) G-jitter-induced motion of a protein crystal under microgravity. J Cryst Growth 294(2):373–384
Smirnova EA, Kislitsyn YA, Sosfenov NI, Lyashenko AV, Popov AN, Baĭdus AN, Timofeev VI, Kuranova IP (2009) Protein crystal growth on the Russian segment of the International Space Station. Crystallogr Rep 54(5):901–911. doi:10.1134/s106377450905023x
Stapelmann J, Smolik G, Lautenschlager P, Lork W, Pletser V (2001) Towards protein crystal growth on the International Space Station (ISS)—Innovative tools, diagnostics and applications. J Cryst Growth 232(1):468–472
Strelov VI, Kuranova IP, Zakharov BG, Voloshin AE (2014) Crystallization in space: results and prospects. Crystallogr Rep 59(6):781–806. doi:10.1134/s1063774514060285
Takahashi S, Ohta K, Furubayashi N, Yan B, Koga M, Wada Y, Yamada M, Inaka K, Tanaka H, Miyoshi H (2013) JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals. J Synchrotron Radiat 20(6):968–973
Tanaka H, Takahashi S, Yamanaka M, Yoshizaki I, Sato M, Sano S, Motohara M, Kobayashi T, Yoshitomi S, Tanaka T (2006) Diffusion coefficient of the protein in various crystallization solutions: the key to growing high-quality crystals in space. Microgravity Sci Technol 18(3):91–94
Tanaka H, Umehara T, Inaka K, Takahashi S, Shibata R, Bessho Y, Sato M, Sugiyama S, Fusatomi E, Terada T, Shirouzu M, Sano S, Motohara M, Kobayashi T, Tanaka T, Tanaka A, Yokoyama S (2007) Crystallization of the archaeal transcription termination factor NusA: a significant decrease in twinning under microgravity conditions. Acta Crystallogr Sect F: Struct Biol Cryst Commun 63(pt 2):69–73. doi:10.1107/S1744309106054625
Tanaka H, Tsurumura T, Aritake K, Furubayashi N, Takahashi S, Yamanaka M, Hirota E, Sano S, Sato M, Kobayashi T, Tanaka T, Inaka K, Urade Y (2011) Improvement in the quality of hematopoietic prostaglandin D synthase crystals in a microgravity environment. J Synchrotron Radiat 18(1):88–91. doi:10.1107/s0909049510037076
Timofeev VI, Smirnova EA, Chupova LA, Esipov RS, Kuranova IP (2010) Preparation of the crystal complex of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis with coenzyme A and investigation of its three-dimensional structure at 2.1-Å resolution. Crystallogr Rep 55(6):1050–1059. doi:10.1134/s1063774510060234
Timofeev V, Smirnova E, Chupova L, Esipov R, Kuranova I (2012a) X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction. Acta Crystallogr D Biol Crystallogr 68(pt 12):1660–1670. doi:10.1107/s0907444912040206
Timofeev VI, Smirnova EA, Chupova LA, Esipov RS, Kuranova IP (2012b) Three-dimensional structure of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis in the apo form and in complexes with coenzyme A and dephosphocoenzyme A. Crystallogr Rep 57(1):96–104. doi:10.1134/s1063774512010142
Timofeev VI, Abramchik YA, Fateev IV, Zhukhlistova NE, Murav’eva TI, Kuranova IP, Esipov RS (2013a) Three-dimensional structure of thymidine phosphorylase from E. coli in complex with 3′-azido-2′-fluoro-2′,3′-dideoxyuridine. Crystallogr Rep 58(6):842–853. doi:10.1134/s1063774513060230
Timofeev VI, Kuznetsov SA, Akparov VK, Chestukhina GG, Kuranova IP (2013b) Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine. Biochem Mosc 78(3):252–259. doi:10.1134/s0006297913030061
Timofeev VI, Abramchik YA, Zhukhlistova NE, Muravieva TI, Esipov RS, Kuranova IP (2016) Three-dimensional structure of phosphoribosyl pyrophosphate synthetase from E. coli at 2.71 Å resolution. Crystallogr Rep 61(1):44–54. doi:10.1134/s1063774516010247
Vahedi-Faridi A, Porta J, Borgstahl GE (2003) Improved three-dimensional growth of manganese superoxide dismutase crystals on the International Space Station. Acta Crystallogr D Biol Crystallogr 59(pt 2):385–388
Vallazza M, Banumathi S, Perbandt M, Moore K, DeLucas L, Betzel C, Erdmann VA (2002) Crystallization and structure analysis of Thermus flavus 5S rRNA helix B. Acta Crystallogr D Biol Crystallogr 58:1700–1703
Vergara A, Corvino E, Sorrentino G, Piccolo C, Tortora A, Carotenuto L, Mazzarella L, Zagari A (2002) Crystallization of the collagen-like polypeptide (PPG) 10 aboard the International Space Station. 1. Video observation. Acta Crystallogr D Biol Crystallogr 58(10):1690–1694
Yoshida H, Yoshihara A, Ishii T, Izumori K, Kamitori S (2016) X-ray structures of the Pseudomonas cichorii D-tagatose 3-epimerase mutant form C66S recognizing deoxy sugars as substrates. Appl Microbiol Biotechnol 100(24):10403–10415. doi:10.1007/s00253-016-7673-7
Yoshikawa S, Kukimoto-Niino M, Parker L, Handa N, Terada T, Fujimoto T, Terazawa Y, Wakiyama M, Sato M, Sano S (2013) Structural basis for the altered drug sensitivities of non-small cell lung cancer-associated mutants of human epidermal growth factor receptor. Oncogene 32(1):27–38
Yoshizaki I, Nakamura H, Fukuyama S, Yoda S, Komatsu H (2004) Scientific approach on the optimization of protein crystallization condition for microgravity experiments. Ann N Y Acad Sci 1027:28–47
Yoshizaki I, Tsukamoto K, Yamazaki T, Murayama K, Oshi K, Fukuyama S, Shimaoka T, Suzuki Y, Tachibana M (2013) Growth rate measurements of lysozyme crystals under microgravity conditions by laser interferometry. Rev Sci Instrum 84:1037072–1037078
Zegers I, Carotenuto L, Evrard C, Garcia-Ruiz J, De Gieter P, Gonzales-Ramires L, Istasse E, Legros J-C, Martial J, Minetti C (2006) Counterdiffusion protein crystallisation in microgravity and its observation with PromISS (Protein Microscope for the International Space Station). Microgravity Sci Technol 18(3):165–169
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
Copyright information
© 2017 The Author(s)
About this chapter
Cite this chapter
Betzel, C., Martirosyan, A., Ruyters, G. (2017). Protein Crystallization on the International Space Station ISS. In: Biotechnology in Space. SpringerBriefs in Space Life Sciences. Springer, Cham. https://doi.org/10.1007/978-3-319-64054-9_3
Download citation
DOI: https://doi.org/10.1007/978-3-319-64054-9_3
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-64053-2
Online ISBN: 978-3-319-64054-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)