title: Diffraction grade crystals of Escherichia coli serine hydroxymethyltransferase.
abstract: Diffraction grade crystals of serine hydroxymethyltransferase were obtained after extensive screening of source of enzyme, purification procedures, ligand binding and crystallization conditions. Serine hydroxymethyltransferase purified from Escherichia coli crystallizes in two forms that are suitable for crystal structure determination.
authors: Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond 23298-0614.
authors: P
authors: P
authors: Stover
authors: H
authors: H
authors: Kruschwitz
authors: V
authors: V
authors: Schirch
authors: H T
authors: HT
authors: Wright
mesh_terms: D000818:Animals; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D012696:Glycine Hydroxymethyltransferase / Q000737:chemistry* / Q000302:isolation & purification; D011817:Rabbits; D014961:X-Ray Diffraction
chemical_list: D012696:Glycine Hydroxymethyltransferase