Crystallization and preliminary X-ray diffraction studies of methyl-coenzyme M reductase from methanobacterium thermoautotrophicum.
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.
Shima
S
S
Max-Planck-Institut für Terrestrische Mikrobiologie and Laboratorium für Mikrobiologie der Phillips-Universität, Marburg, Germany.
Goubeaud
M
M
Vinzenz
D
D
Thauer
R K
RK
Ermler
U
U
D003460:Crystallization; D018360:Crystallography, X-Ray; D017014:Methanobacterium / Q000201:enzymology*; D015394:Molecular Structure; D010088:Oxidoreductases / Q000737:chemistry*
D010088:Oxidoreductases; C021572:methyl coenzyme M reductase