Purification and crystallization of the hydroxylase component of the methanesulfonate monooxygenase from Methylosulfonomonas methylovora strain M2.

Authors :: Jamshad M
Murrell JC
Fülöp V
Source :: Protein expression and purification [Protein Expr Purif] 2007 Apr; Vol. 52 (2), pp. 472-7. Date of Electronic Publication: 2006 Nov 09.
Publication Year :: 2007
Abstract: The aim of the work described in this paper was two-fold: (1) the purification of the hydroxylase component of the MSAMO to electrophoretic homogeneity using a four-step chromatographic strategy and (2) the crystallization of the two-component hydroxylase of the MSAMO in order to enhance our understanding of the precise three-dimensional structure of the MSAMO, thus yielding an insight into the nature of the active site of this enzyme. Optimised crystallization conditions were identified allowing growth of crystals of the hydroxylase component of the MSAMO within five days. Crystals exhibited a brown colour suggesting the presence on an intact Rieske-iron sulfur centre and diffracted to 7.0A when a few degrees of data were evaluated on a beam line X11.

Subjects :: Amino Acid Sequence
Crystallization
Mesylates metabolism
Mixed Function Oxygenases chemistry
Mixed Function Oxygenases metabolism
Molecular Sequence Data
Protein Conformation
Sequence Analysis, Protein
Alphaproteobacteria enzymology
Mixed Function Oxygenases isolation & purification
Protein Subunits isolation & purification

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