Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA.
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.
Bent
Colin J
CJ
Department of Chemistry, University of Glasgow, Scotland.
Isaacs
Neil W
NW
Mitchell
Timothy J
TJ
Riboldi-Tunnicliffe
Alan
A
D003001:Cloning, Molecular; D003460:Crystallization; D015395:Histocompatibility Antigens Class I / Q000096:biosynthesis* / Q000737:chemistry* / Q000302:isolation & purification; D010957:Plasmids / Q000235:genetics; D013296:Streptococcus pneumoniae / Q000737:chemistry* / Q000235:genetics*; D014961:X-Ray Diffraction
D015395:Histocompatibility Antigens Class I; C099187:MHC class I-related chain A