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. 2009 Jun 1;65(Pt 6):574-6.
doi: 10.1107/S1744309109014833. Epub 2009 May 22.

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

Lin Wang  1 , Haipeng Wang, Jianbin Ruan, Changlin Tian, Baolin Sun, Jianye Zang
Affiliations

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

Lin Wang et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

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.

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Figures

Figure 1
Figure 1
SDS–PAGE analysis of the purification of Sa239. Lane 1, markers (kDa); lane 2, cell lysate; lane 3, eluant from Ni–NTA nickel-chelating column; lane 4, SUMO-Sa239 cleaved by SUMO protease; lane 5: the flowthrough fraction after passage of the SA239 and SUMO mixture through the second Ni–NTA nickel-chelating column; lane 6: eluted fraction containing Sa239 from the HiLoad 16/60 Superdex 200 size-exclusion column.
Figure 2
Figure 2
Crystal of Sa239.
Figure 3
Figure 3
X-ray diffraction frame collected from a crystal of Sa239.
See this image and copyright information in PMC

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