title: 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.
authors.affiliation: Lehrstuhl für Biotechnik, Department of Biology, Friederich-Alexander University Erlangen-Nuremberg, Erlangen, Germany.
authors.forename: Marcus
authors.initials: M
authors.lastname: Resch
authors.forename: Heide Marie
authors.initials: HM
authors.lastname: Roth
authors.forename: Mathias
authors.initials: M
authors.lastname: Kottmair
authors.forename: Madhumati
authors.initials: M
authors.lastname: Sevvana
authors.forename: Ralph
authors.initials: R
authors.lastname: Bertram
authors.forename: Fritz
authors.initials: F
authors.lastname: Titgemeyer
authors.forename: Yves A
authors.initials: YA
authors.lastname: Muller