Crystallization and preliminary X-ray analysis of CrgA, a LysR-type transcriptional regulator from pathogenic Neisseria meningitidis MC58
AUTOR(ES)
Sainsbury, Sarah
FONTE
International Union of Crystallography
RESUMO
The full length and the regulatory domain of the LysR-type transcriptional regulator CrgA have been crystallized. Diffraction data were collected from two crystal forms of full-length CrgA to 3.0 and 3.8 Å resolution, respectively. Crystals of the selenomethionine derivative of the C-terminal regulatory domain of CrgA diffracted to 2.3 Å resolution.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2531262Documentos Relacionados
- Intimate adhesion of Neisseria meningitidis to human epithelial cells is under the control of the crgA gene, a novel LysR-type transcriptional regulator
- Crystallization and preliminary X-ray diffraction analysis of GCIP/HHM transcriptional regulator
- Analysis of DNA Binding and Transcriptional Activation by the LysR-Type Transcriptional Regulator CbbR of Xanthobacter flavus
- Crystallization and preliminary X-ray analysis of endoglucanase from Pyrococcus horikoshii
- Crystallization and preliminary X-ray analysis of glutathione transferases from cyanobacteria
