Purification of component A of the soluble methane monooxygenase of Methylococcus capsulatus (Bath) by high-pressure gel permeation chromatography
โ Scribed by Marc P. Woodland; Howard Dalton
- Publisher
- Elsevier Science
- Year
- 1984
- Tongue
- English
- Weight
- 510 KB
- Volume
- 139
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
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 is enhanced and more importantly the recovered protein displays an increased specific activity, unlike that purified by other techniques.
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