Open AccessCloning, purification, crystallization and preliminary crystallographic analysis of a ribokinase from Staphylococcus aureus
Author(s) -
Wang Lin,
Wang Haipeng,
Ruan Jianbin,
Tian Changlin,
Sun Baolin,
Zang Jianye
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109014833
Subject(s) - crystallization , staphylococcus aureus , crystallography , ribose , molecule , chemistry , crystal structure , resolution (logic) , cloning (programming) , stereochemistry , materials science , biology , biochemistry , bacteria , genetics , organic chemistry , artificial intelligence , computer science , programming language , enzyme
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 Å resolution and belonged to space group P 6 1 22 or P 6 5 22, with unit‐cell parameters a = b = 91.8, c = 160.7 Å. Preliminary crystallographic analysis revealed that the Matthews coefficient V M was 3.01 Å 3 Da −1 , indicating the presence of one molecule in the asymmetric unit.