Crystallization and Preliminary X-Ray Diffraction Studies of Methyl-Coenzyme M Reductase from Methanobacterium thermoautotrophicum
- 1 May 1997
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 121 (5) , 829-830
- https://doi.org/10.1093/oxfordjournals.jbchem.a021660
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 P21, with unit cell parameters of a=83.2 Å, b=117.4 Å, c=125.lÅ, and β=92.6., and diffracted at better than 2.8 Å resolution. Crystal form P grown from polyethylene glycol 400 belonged to space group P21, and had unit cell parameters of a=83.1 Å, b=120.2 Å, c=123.1 Å, and β=91.7., diffracting at least to 1.7 Å resolution. Both crystal forms have one molecule per asymmetric unit and are suitable for X-ray structure analysis.Keywords
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