Protein crystal growth on board Shenzhou 3: a concerted effort improves crystal diffraction quality and facilitates structure determination.
The crystallization of 16 proteins was carried out using 60 wells on board Shenzhou 3 in 2002. Although the mission was only 7 days, careful and concerted planning at all stages made it possible to obtain crystals of improved quality compared to their ground controls for some of the proteins. Significantly improved resolutions were obtained from diffracted crystals of 4 proteins. A complete data set from a space crystal of the PEP carboxykinase yielded significantly higher resolution (1.46A vs. 1.87A), I/sigma (22.4 vs. 15.5), and a lower average temperature factor (29.2A(2) vs. 42.9A(2)) than the best ground-based control crystal. The 3-D structure of the enzyme is well improved with significant ligand density. It has been postulated that the reduced convection and absence of macromolecule sedimentation under microgravity have advantages/benefits for protein crystal growth. Improvements in experimental design for protein crystal growth in microgravity are ongoing.
Han
Y
Y
Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Cang
H-X
HX
Zhou
J-X
JX
Wang
Y-P
YP
Bi
R-C
RC
Colelesage
J
J
Delbaere
L T J
LT
Nahoum
V
V
Shi
R
R
Zhou
M
M
Zhu
D-W
DW
Lin
S-X
SX
D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D015786:Cytochromes b5 / Q000737:chemistry; D004583:Electrons; D004926:Escherichia coli / Q000201:enzymology; D005583:Fourier Analysis; D006801:Humans; D008958:Models, Molecular; D019764:Phosphoenolpyruvate Carboxykinase (ATP) / Q000737:chemistry; D015398:Signal Transduction; D012984:Software; D013026:Space Flight; D013696:Temperature; D014893:Weightlessness
D015786:Cytochromes b5; D019764:Phosphoenolpyruvate Carboxykinase (ATP)