Purification and crystallization of the hydroxylase component of the methanesulfonate monooxygenase from Methylosulfonomonas methylovora strain M2.
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.
Jamshad
Mohammed
M
Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK. m.jamshad@aston.ac.uk
Murrell
J Colin
JC
Fülöp
Vilmos
V
D020561:Alphaproteobacteria / Q000201:enzymology*; D000595:Amino Acid Sequence; D003460:Crystallization; D008698:Mesylates / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D021122:Protein Subunits / Q000302:isolation & purification*; D020539:Sequence Analysis, Protein
D008698:Mesylates; D021122:Protein Subunits; C045880:methanesulfonic acid; D006899:Mixed Function Oxygenases