Jamshad, Mohammed, Murrell, J. C. (J. Colin) and Fulop, Vilmos. (2007) Purification and crystallization of the hydroxylase component of the methanesulfonate monooxygenase from Methylosulfonomonas methylovora strain M2. Protein Expression and Purification, Vol.52 (No.2). pp. 472-477. ISSN 1046-5928

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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 7.0 angstrom when a few degrees of data were evaluated on a beam line X11. (c) 2006 Elsevier Inc. All rights reserved.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry T Technology > TP Chemical technology
Divisions:	Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Journal or Publication Title:	Protein Expression and Purification
Publisher:	Academic Press
ISSN:	1046-5928
Date:	April 2007
Volume:	Vol.52
Number:	No.2
Number of Pages:	6
Page Range:	pp. 472-477
Identification Number:	10.1016/j.pep.2006.11.001
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
URI:	http://wrap.warwick.ac.uk/id/eprint/32119

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