title: Crystallization and preliminary crystallographic analysis of human serine dehydratase.
abstract: L-Serine dehydratase (SDH) catalyzes the pyridoxal phosphate (PLP) dependent deamination of L-serine to yield pyruvate. Recombinant human serine dehydratase was crystallized by the hanging-drop vapour-diffusion method. Crystals were grown at 291 K using (NH4)(2)SO4 as precipitant. Diffraction data were obtained to a resolution of 2.5 A from a single frozen crystal using Cu Kalpha radiation. The crystal belongs to space group I422, with unit-cell parameters a = 157.4, b = 157.4, c = 59.2 A, alpha = beta = gamma = 90 degrees. The asymmetric unit contains one molecule and has a solvent content of about 46%.
authors.affiliation: MOE Protein Science Laboratory and Laboratory of Structural Biology, Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, People's Republic of China.
authors.forename: Lei
authors.initials: L
authors.lastname: Sun
authors.forename: Xuemei
authors.initials: X
authors.lastname: Li
authors.forename: Yanjie
authors.initials: Y
authors.lastname: Dong
authors.forename: Maojun
authors.initials: M
authors.lastname: Yang
authors.forename: Yiwei
authors.initials: Y
authors.lastname: Liu
authors.forename: Xueqing
authors.initials: X
authors.lastname: Han
authors.forename: Xianen
authors.initials: X
authors.lastname: Zhang
authors.forename: Hai
authors.initials: H
authors.lastname: Pang
authors.forename: Zihe
authors.initials: Z
authors.lastname: Rao
mesh_terms: D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006801:Humans; D012695:L-Serine Dehydratase / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D011994:Recombinant Proteins; D012695:L-Serine Dehydratase