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

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

Content Provider	Europe PMC
Author	Wang, Lin Wang, Haipeng Ruan, Jianbin Tian, Changlin Sun, Baolin Zang, Jianye
Copyright Year	2009
Description	The ribokinase Sa239 from S. aureus has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.9 Å resolution. 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 P6122 or P6522, 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 Å3 Da−1, indicating the presence of one molecule in the asymmetric unit.
Related Links	https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC2688413&blobtype=pdf
Volume Number	65
PubMed Central reference number	PMC2688413
Issue Number	Pt 6
Issue Number	pt 6
PubMed reference number	19478434
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications [Acta Crystallogr Sect F Struct Biol Cryst Commun]
e-ISSN	17443091
DOI	10.1107/s1744309109014833
Language	English
Publisher	International Union of Crystallography
Publisher Date	2009-05-22
Access Restriction	Open
Rights License	© International Union of Crystallography 2009
Subject Keyword	ribokinase Sa239 Staphylococcus aureus
Content Type	Text
Resource Type	Article
Subject	Biochemistry Condensed Matter Physics Genetics Biophysics Structural Biology

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