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

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 A resolution and belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 91.8, c = 160.7 A. Preliminary crystallographic analysis revealed that the Matthews coefficient V(M) was 3.01 A(3) Da(-1), indicating the presence of one molecule in the asymmetric unit.

Citation

Lin Wang, Haipeng Wang, Jianbin Ruan, Changlin Tian, Baolin Sun, Jianye Zang. Cloning, purification, crystallization and preliminary crystallographic analysis of a ribokinase from Staphylococcus aureus. Acta crystallographica. Section F, Structural biology and crystallization communications. 2009 Jun 01;65(Pt 6):574-6

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PMID: 19478434

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