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  • Title: Crystallization and preliminary X-ray diffraction studies of methyl-coenzyme M reductase from methanobacterium thermoautotrophicum.
    Author: Shima S, Goubeaud M, Vinzenz D, Thauer RK, Ermler U.
    Journal: J Biochem; 1997 May; 121(5):829-30. PubMed ID: 9192720.
    Abstract:
    Methyl-coenzyme M reductase isoenzyme I from the methanogenic Archaeon, Methanobacterium thermoautotrophicum (strain Marburg), was crystallized by vapor diffusion methods. Crystal form M obtained with 2-methyl-2,4-pentanediol as the precipitant displayed space group P2(1), with unit cell parameters of a=83.2 A, b=117.4 A, c=125.1 A, and beta= 92.6 degrees, and diffracted at better than 2.8 A resolution. Crystal form P grown from polyethylene glycol 400 belonged to space group P2(1), and had unit cell parameters of a=83.1 A, b=120.2 A, c=123.1 A, and beta=91.7 degrees, diffracting at least to 1.7 A resolution. Both crystal forms have one molecule per asymmetric unit and are suitable for X-ray structure analysis.
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