PMID:1593636
| Citation |
Luschinsky, CL, Drummond, JT, Matthews, RG and Ludwig, ML (1992) Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli. J. Mol. Biol. 225:557-60 |
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| 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. |
| Links | |
| Keywords |
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/chemistry; 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/metabolism; Amino Acid Sequence; Binding Sites; Crystallization; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Methylation; Molecular Sequence Data; Vitamin B 12/metabolism; X-Ray Diffraction |
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