Purification and crystallization of the hydroxylase component of the methanesulfonate monooxygenase from Methylosulfonomonas methylovora strain M2
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 1046-5928Full text not available from this repository.
Official URL: http://dx.doi.org/10.1016/j.pep.2006.11.001
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|
|Official Date:||April 2007|
|Number of Pages:||6|
|Page Range:||pp. 472-477|
|Access rights to Published version:||Restricted or Subscription Access|
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