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Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA.
- Source :
-
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2003 Apr; Vol. 59 (Pt 4), pp. 758-60. Date of Electronic Publication: 2003 Mar 25. - Publication Year :
- 2003
-
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.
- Subjects :
- Cloning, Molecular
Crystallization
Histocompatibility Antigens Class I isolation & purification
Plasmids genetics
X-Ray Diffraction
Histocompatibility Antigens Class I biosynthesis
Histocompatibility Antigens Class I chemistry
Streptococcus pneumoniae chemistry
Streptococcus pneumoniae genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0907-4449
- Volume :
- 59
- Issue :
- Pt 4
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section D, Biological crystallography
- Publication Type :
- Academic Journal
- Accession number :
- 12657804
- Full Text :
- https://doi.org/10.1107/s090744490300372x