Purification, crystallization and preliminary X-ray analysis of apo glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from methicillin-resistant Staphylococcus aureus (MRSA252)

被引：2
|
作者：
Mukherjee, Somnath [1 ]
Saha, Baisakhee [1 ]
Dutta, Debajyoti [1 ]
Das, Amit Kumar [1 ]
机构：
[1] Indian Inst Technol, Dept Biotechnol, Kharagpur 721302, W Bengal, India
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
关键词：
TRANSFERRIN-BINDING; CANDIDA-ALBICANS; PROTEIN; DIFFRACTION; SITE;
D O I：
10.1107/S1744309110007980
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from methicillin-resistant Staphylococcus aureus (MRSA252) has been purified to homogeneity in the apo form. The protein was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group P2(1), with unit-cell parameters a = 69.95, b = 93.68, c = 89.05 angstrom, beta = 106.84 degrees. X-ray diffraction data have been collected and processed to a maximum resolution of 2.2 angstrom. The presence of one tetramer in the asymmetric unit gives a Matthews coefficient (V-M) of 1.81 angstrom(3) Da(-1) with a solvent content of 32%. The structure has been solved by molecular replacement and structure refinement is now in progress.
引用
收藏
页码：506 / 508
页数：3
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