Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA

Colin J Bent; Neil W Isaacs; Timothy J Mitchell; Alan Riboldi-Tunnicliffe

Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA

Colin J Bent, Neil W Isaacs, Timothy J Mitchell, Alan Riboldi-Tunnicliffe

Microbiology and Infection

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

3 Citations (Scopus)

Abstract

MicA is a response regulator from Streptococcus pneumoniae thought to be involved in redox-energy sensing under oxygen-limiting environments. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. X-ray diffraction data were collected using synchrotron radiation to a resolution of 1.91 A. The crystals belong to the monoclinic space group C222(1), with unit-cell parameters a = 78.69, b = 92.57, c = 37.16 A, alpha = beta = gamma = 90.0 degrees. The Matthews coefficient indicates that MicA crystallizes with one molecule in the asymmetric unit.

Original language	English
Pages (from-to)	758-60
Number of pages	3
Journal	Acta Crystallographica Section D Biological Crystallography
Volume	59
Issue number	Pt 4
Publication status	Published - Apr 2003

Keywords

Cloning, Molecular
Crystallization
Histocompatibility Antigens Class I
Plasmids
Streptococcus pneumoniae
X-Ray Diffraction

Cite this

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title = "Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA",

abstract = "MicA is a response regulator from Streptococcus pneumoniae thought to be involved in redox-energy sensing under oxygen-limiting environments. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. X-ray diffraction data were collected using synchrotron radiation to a resolution of 1.91 A. The crystals belong to the monoclinic space group C222(1), with unit-cell parameters a = 78.69, b = 92.57, c = 37.16 A, alpha = beta = gamma = 90.0 degrees. The Matthews coefficient indicates that MicA crystallizes with one molecule in the asymmetric unit.",

keywords = "Cloning, Molecular, Crystallization, Histocompatibility Antigens Class I, Plasmids, Streptococcus pneumoniae, X-Ray Diffraction",

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pages = "758--60",

journal = "Acta Crystallographica Section D Biological Crystallography",

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T1 - Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA

AU - Bent, Colin J

AU - Isaacs, Neil W

AU - Mitchell, Timothy J

AU - Riboldi-Tunnicliffe, Alan

PY - 2003/4

Y1 - 2003/4

N2 - MicA is a response regulator from Streptococcus pneumoniae thought to be involved in redox-energy sensing under oxygen-limiting environments. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. X-ray diffraction data were collected using synchrotron radiation to a resolution of 1.91 A. The crystals belong to the monoclinic space group C222(1), with unit-cell parameters a = 78.69, b = 92.57, c = 37.16 A, alpha = beta = gamma = 90.0 degrees. The Matthews coefficient indicates that MicA crystallizes with one molecule in the asymmetric unit.

AB - MicA is a response regulator from Streptococcus pneumoniae thought to be involved in redox-energy sensing under oxygen-limiting environments. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. X-ray diffraction data were collected using synchrotron radiation to a resolution of 1.91 A. The crystals belong to the monoclinic space group C222(1), with unit-cell parameters a = 78.69, b = 92.57, c = 37.16 A, alpha = beta = gamma = 90.0 degrees. The Matthews coefficient indicates that MicA crystallizes with one molecule in the asymmetric unit.

KW - Cloning, Molecular

KW - Crystallization

KW - Histocompatibility Antigens Class I

KW - Plasmids

KW - Streptococcus pneumoniae

KW - X-Ray Diffraction

M3 - Article

C2 - 12657804

SN - 0907-4449

VL - 59

SP - 758

EP - 760

JO - Acta Crystallographica Section D Biological Crystallography

JF - Acta Crystallographica Section D Biological Crystallography

IS - Pt 4

ER -

Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA

Abstract

Keywords

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