Crystallization and preliminary crystallographic analysis of human serine dehydratase.

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Sun L, Li X, Dong Y, Yang M, Liu Y, Han X, Zhang X, Pang H, Rao Z

Crystallization and preliminary crystallographic analysis of human serine dehydratase.

Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2297-9. Epub 2003 Nov 27.

PubMed ID

14646100 [ View in PubMed

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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%.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Pyridoxal phosphate	L-serine dehydratase/L-threonine deaminase	Protein	Humans	Unknown	Cofactor	Details

Polypeptides

Name	UniProt ID
L-serine dehydratase/L-threonine deaminase	P20132	Details