Mechanistic studies of methane monooxygenase from Methylococcus capsulatus (Bath).
โ Scribed by K.E. Liu; A. Masschelein; S.J. Lippard
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 63 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0162-0134
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๐ SIMILAR VOLUMES
The crystal structure of the nonheme iron-containing hydroxylase component of methane monooxygenase hydroxylase (MMOH) from Methylococcus capsulatus (Bath) has been solved in two crystal forms, one of which was refined to 1.7 ร resolution. The enzyme is composed of two copies each of three subunits
A major improvement in the purification of the oxygenase protein (component A) of the methane monooxygenase has been effected. By employing high-pressure gel permeation chromatography several purification steps may be omitted from the previously published scheme. Furthermore the yield of the protein