title: Crystallization and preliminary X-ray crystallographic analysis of d-phenylglycine aminotransferase from Pseudomonas stutzeri ST201.
abstract: d-Phenylglycine aminotransferase (d-PhgAT) catalyzes the reversible transamination of d-phenylglycine to l-glutamate with 2-oxoglutarate as the amino-group acceptor. Crystals of substrate-free Pseudomonas stutzeri d-PhgAT bound to the cofactor pyridoxal-5'-phosphate (PLP) were obtained by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 75.155, c = 147.554 A. The asymmetric unit contains one molecule of d-PhgAT and has a solvent content of 50.0%. A complete native X-ray diffraction data set was collected from a single crystal at 100 K to a resolution of 2.3 A.
authors.affiliation: Department of Chemistry, Faculty of Science, Mahidol University, Rama VI Road, Bangkok 10400, Thailand. scpks@mahidol.ac.th
authors.forename: Palangpon
authors.initials: P
authors.lastname: Kongsaeree
authors.forename: Chariwat
authors.initials: C
authors.lastname: Samanchart
authors.forename: Poramaet
authors.initials: P
authors.lastname: Laowanapiban
authors.forename: Suthep
authors.initials: S
authors.lastname: Wiyakrutta
authors.forename: Vithaya
authors.initials: V
authors.lastname: Meevootisom
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D044223:Pseudomonas stutzeri / Q000201:enzymology* / Q000235:genetics; D011732:Pyridoxal Phosphate / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D000637:Transaminases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D011732:Pyridoxal Phosphate; C108039:D-phenylglycine aminotransferase; D000637:Transaminases