Literature DB >> 19478434

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

Lin Wang1, Haipeng Wang, Jianbin Ruan, Changlin Tian, Baolin Sun, Jianye Zang.   

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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Year:  2009        PMID: 19478434      PMCID: PMC2688413          DOI: 10.1107/S1744309109014833

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  9 in total

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Journal:  Methods Enzymol       Date:  1997       Impact factor: 1.600

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Journal:  Bioorg Med Chem       Date:  2006-06-19       Impact factor: 3.641

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Journal:  J Mol Biol       Date:  2002-01-18       Impact factor: 5.469

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Authors:  M C Maj; R S Gupta
Journal:  J Protein Chem       Date:  2001-02

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Journal:  Structure       Date:  1998-02-15       Impact factor: 5.006

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Journal:  J Bacteriol       Date:  1984-05       Impact factor: 3.490

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Authors:  P Bork; C Sander; A Valencia
Journal:  Protein Sci       Date:  1993-01       Impact factor: 6.725

  9 in total

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