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Studies of the hydroxylase component of soluble methane monooxygenase from Methylococcus capsulatus (Bath)

✍ Scribed by Y. Jiang; P.C. Wilkins; H. Dalton

Publisher
Elsevier Science
Year
1993
Tongue
English
Weight
96 KB
Volume
51
Category
Article
ISSN
0162-0134

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πŸ“œ SIMILAR VOLUMES

Crystal structures of the methane monoox
Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): Implications for substrate gating and component interactions
✍ Amy C. Rosenzweig; Hans Brandstetter; Douglas A. Whittington; PΓ€r Nordlund; Step πŸ“‚ Article πŸ“… 1997 πŸ› John Wiley and Sons 🌐 English βš– 386 KB

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 Γ… resolution. The enzyme is composed of two copies each of three subunits

Purification of component A of the solub
Purification of component A of the soluble methane monooxygenase of Methylococcus capsulatus (Bath) by high-pressure gel permeation chromatography
✍ Marc P. Woodland; Howard Dalton πŸ“‚ Article πŸ“… 1984 πŸ› Elsevier Science 🌐 English βš– 510 KB

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