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

Mohammed Jamshad; J. Colin Murrell; Vilmos Fulop

doi:10.1016/j.pep.2006.11.001

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

Mohammed Jamshad^*, J. Colin Murrell, Vilmos Fulop

^*Corresponding author for this work

School of Biosciences

Research output: Contribution to journal › Article › peer-review

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 Å when a few degrees of data were evaluated on a beam line X11. © 2006 Elsevier Inc. All rights reserved.

Original language	English
Pages (from-to)	472-477
Number of pages	6
Journal	Protein Expression and Purification
Volume	52
Issue number	2
DOIs	https://doi.org/10.1016/j.pep.2006.11.001
Publication status	Published - Apr 2007

Keywords

crystallization
hydroxylase
methanesulfonate monooxygenase
purification

Access to Document

10.1016/j.pep.2006.11.001

Cite this

@article{6aad88e602c34238b4ea0efe1afcda95,

title = "Purification and crystallization of the hydroxylase component of the methanesulfonate monooxygenase from Methylosulfonomonas methylovora strain M2",

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 {\AA} when a few degrees of data were evaluated on a beam line X11. {\textcopyright} 2006 Elsevier Inc. All rights reserved.",

keywords = "crystallization, hydroxylase, methanesulfonate monooxygenase, purification",

author = "Mohammed Jamshad and Murrell, {J. Colin} and Vilmos Fulop",

year = "2007",

month = apr,

doi = "10.1016/j.pep.2006.11.001",

language = "English",

volume = "52",

pages = "472--477",

journal = "Protein Expression and Purification",

issn = "1046-5928",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - Purification and crystallization of the hydroxylase component of the methanesulfonate monooxygenase from Methylosulfonomonas methylovora strain M2

AU - Jamshad, Mohammed

AU - Murrell, J. Colin

AU - Fulop, Vilmos

PY - 2007/4

Y1 - 2007/4

N2 - 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 Å when a few degrees of data were evaluated on a beam line X11. © 2006 Elsevier Inc. All rights reserved.

AB - 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 Å when a few degrees of data were evaluated on a beam line X11. © 2006 Elsevier Inc. All rights reserved.

KW - crystallization

KW - hydroxylase

KW - methanesulfonate monooxygenase

KW - purification

UR - http://www.scopus.com/inward/record.url?scp=33846446390&partnerID=8YFLogxK

U2 - 10.1016/j.pep.2006.11.001

DO - 10.1016/j.pep.2006.11.001

M3 - Article

C2 - 17169571

SN - 1046-5928

VL - 52

SP - 472

EP - 477

JO - Protein Expression and Purification

JF - Protein Expression and Purification

IS - 2

ER -

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this