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

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 Å resolution. The crystals belonged to the monoclinic space group C 2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecules per asymmetric unit.