title: Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli.
abstract: Crystals of a cobalamin-binding domain (M(r) = 28,000) have been grown in polyethylene glycol 6000 at pH 7.5, starting from solutions of intact (M(r) = 133,000) cobalamin-dependent methionine synthase. The crystals are orthorhombic in space group P2(1)2(1)2(1), with cell dimensions a = 96.9 A, b = 55.4 A, c = 103.8 A. For two molecules per asymmetric unit, the calculated VM value is 2.45 A3/Da. A native data set has been collected to 3 A resolution.
authors.affiliation: Biophysics Research Division, University of Michigan, Ann Arbor 48109-2099.
authors.forename: C L
authors.initials: CL
authors.lastname: Luschinsky
authors.forename: J T
authors.initials: JT
authors.lastname: Drummond
authors.forename: R G
authors.initials: RG
authors.lastname: Matthews
authors.forename: M L
authors.initials: ML
authors.lastname: Ludwig
mesh_terms: D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008745:Methylation; D008969:Molecular Sequence Data; D014805:Vitamin B 12 / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase; D014805:Vitamin B 12