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Crystallization and preliminary X-ray diffraction studies of methyl-coenzyme M reductase from methanobacterium thermoautotrophicum

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Shima,  Seigo
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Goubeaud,  Marcel
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons252235

Vinzenz,  Daniela
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons254760

Thauer,  Rudolf Kurt
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons137648

Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Shima, S., Goubeaud, M., Vinzenz, D., Thauer, R. K., & Ermler, U. (1997). Crystallization and preliminary X-ray diffraction studies of methyl-coenzyme M reductase from methanobacterium thermoautotrophicum. Journal of Biochemistry, 121(5), 829-830. doi:10.1093/oxfordjournals.jbchem.a021660.


Cite as: https://hdl.handle.net/21.11116/0000-0009-4B44-7
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 P21, 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.