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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of YvoA from Bacillus subtilis.

ABSTRACT: The putative transcriptional regulator protein YvoA (BSU35030) from Bacillus subtilis was cloned and heterologously expressed in Escherichia coli. The protein was purified by immobilized metal-affinity chromatography and size-exclusion chromatography and subsequently crystallized. A complete native data set was collected to 2.50 A resolution. The crystals belonged to the monoclinic space group C2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecules per asymmetric unit.

SUBMITTER: Resch M

PROVIDER: S-EPMC2664774 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of YvoA from Bacillus subtilis.

Resch Marcus M Roth Heide Marie HM Kottmair Mathias M Sevvana Madhumati M Bertram Ralph R Titgemeyer Fritz F Muller Yves A YA

Acta crystallographica. Section F, Structural biology and crystallization communications 20090326 Pt 4

The putative transcriptional regulator protein YvoA (BSU35030) from Bacillus subtilis was cloned and heterologously expressed in Escherichia coli. The protein was purified by immobilized metal-affinity chromatography and size-exclusion chromatography and subsequently crystallized. A complete native data set was collected to 2.50 A resolution. The crystals belonged to the monoclinic space group C2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecule ...[more]

PMID: 19342794

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