Cloning, purification, crystallization and preliminary crystallographic analysis of a ribokinase from Staphylococcus aureus

被引：2
|
作者：
Wang, Lin [1 ,2 ]
Wang, Haipeng [1 ]
Ruan, Jianbin [1 ]
Tian, Changlin [1 ,2 ]
Sun, Baolin [1 ,2 ]
Zang, Jianye [1 ]
机构：
[1] Univ Sci & Technol China, Sch Life Sci, Hefei 230027, Anhui, Peoples R China
[2] Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230027, Anhui, Peoples R China
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2009年 / 65卷
关键词：
ESCHERICHIA-COLI; RIBOSE;
D O I：
10.1107/S1744309109014833
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The gene SA239 from Staphylococcus aureus encodes a ribokinase that catalyzes the phosphorylation of D-ribose to produce ribose-5-phosphate. Sa239 was crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to 2.9 angstrom resolution and belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 91.8, c = 160.7 angstrom. Preliminary crystallographic analysis revealed that the Matthews coefficient V-M was 3.01 angstrom(3) Da(-1), indicating the presence of one molecule in the asymmetric unit.
引用
收藏
页码：574 / 576
页数：3
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