title: Crystallization and preliminary X-ray analysis of phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus.
abstract: Recombinant phosphoserine aminotransferase (EC 2.6.1.52) from Bacillus circulans subsp. alkalophilus was crystallized at room temperature from 0.1 M sodium acetate buffer, pH 4.6, and 2% PEG 20000, using macroseeding techniques. The crystals diffract X-rays to at least 2.0 A nominal resolution. They belong to space group C2 with unit cell dimensions a = 93.2 A, b = 93.1 A, c = 45.6 A, alpha = 90.0 degrees, beta = 106.8 degrees, gamma = 90.0 degrees. A native data set to 2.3 A has been collected. Assuming an average packing density of the crystals, there is one monomer in the asymmetric unit, resulting in a calculated solvent content of 48.2%.
authors.affiliation: Department of Structural Biology, Biozentrum, University of Basel, Switzerland.
authors.forename: M
authors.initials: M
authors.lastname: Moser
authors.forename: R
authors.initials: R
authors.lastname: Müller
authors.forename: N
authors.initials: N
authors.lastname: Battchikova
authors.forename: M
authors.initials: M
authors.lastname: Koivulehto
authors.forename: T
authors.initials: T
authors.lastname: Korpela
authors.forename: J N
authors.initials: JN
authors.lastname: Jansonius
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D018360:Crystallography, X-Ray; D011994:Recombinant Proteins / Q000737:chemistry; D000637:Transaminases / Q000737:chemistry*
chemical_list: D011994:Recombinant Proteins; D000637:Transaminases; C022393:phosphoserine aminotransferase