期刊论文详细信息
FEBS Letters
Crystallization of proteins under microgravity
Betzel, Christian5  Plaas-Link, Andreas1  Düvel, Martina2  Schulz, Georg E.6  Weber, Gabriela8  Erdmann, Volker A.4  Müller, Christoph W.6  Saenger, Wolfram2  Dauter, Zbyszek5  Hinrichs, Winfried2  Liesum, Alexander7  Wittmann, Heinz G.3  Yonath, Ada8  Lippmann, Corinna4  Müller-Fahrnow, Anke2  Hilgenfeld, Rolf7  Hoven, Julia5  Stegen, Karin1  Wilson, Keith5 
[1] Intospace, Prinzenstr. 17, D-3000 Hannover 1, FRG;Institut für Kristallographie. FU, Takustr. 6, D-1000 Berlin 33, Germany;Max-Planck-Institut für molekulare Genetik, Ihnestr. 63-73, D-1000 Berlin 33, Germany;Institut für Biochemie, Thielallee 63, D-1000 Berlin 33, Germany;EMBL c/o DESY, Notkestr. 85, D-2000 Hamburg 52, FRG;Universität Freiburg, Albertstr. 21, D-7800 Freiburg, FRG;Hoechst AG, P.O.B. 800320, D-6230 Frankfurt 80, FRG;Max-Planck-Forschungsgruppe für strukturelle Molekularbiologie c/o DESY, Notkestr. 85, D-2000 Hamburg 52, FRG
关键词: Protein crystallization;    Microgravity;   
DOI  :  10.1016/0014-5793(89)81526-1
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

For the crystallization of proteins under microgravity conditions, a Chinese re-entry system was used, in which 101 experiments of 25 different biological macromolecules were accommodated. From the results obtained we conclude that under microgravity conditions crystal growth can only be expected under those crystallization conditions which also permit crystal growthon earth. A number of space-grown crystals were larger in size and of a better quality in their ability to diffract X-rays than the corresponding ground control crystals grown at the Chinese launch site. However, the space-grown crystals have not reached the X-ray diffraction quality of the crystals obtained under optimal conditions in the home laboratories.

【 授权许可】

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