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Crystallization and preliminary X-ray analysis of CrgA, a LysR-type transcriptional regulator from pathogenic Neisseria meningitidis MC58

DOI: 10.1107/S1744309108024068 DOI Help
PMID: 18765907 PMID Help

Authors: Sarah Sainsbury (University of Oxford) , Jingshan Ren (University of Oxford) , Paul Saunders (University of Hull) , Dave Stuart (Diamond Light Source) , Raymond Owens (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 64 , PAGES 797-801

State: Published (Approved)
Published: September 2008

Abstract: Although LysR-type regulators (LTTRs) represent the largest family of transcriptional regulators in bacteria, the full-length structure of only one annotated LTTR (CbnR) has been deposited in the PDB. CrgA, a LTTR from pathogenic Neisseria meningitidis MC58, which is up-regulated upon bacterial cell contact with human epithelial cells, has been cloned, purified and crystallized. Crystals of full-length CrgA were obtained after buffer screening with a thermal shift assay and concentration with 0.2 M NDSB-256. Data were collected from two crystal forms of full-length CrgA belonging to space groups P212121 and P21, diffracting to 3.0 and 3.8 Å resolution and consistent with the presence of between six and ten and between ten and 20 copies of CrgA in the asymmetric unit, respectively. In addition, diffraction data were collected to 2.3 Å resolution from the selenomethionine derivative of the regulatory domain of CrgA. The crystals belonged to space group P21 and contained two molecules in the asymmetric unit.

Journal Keywords: Crga; Neisseria Meningitidis; Lysr-Type Regulators.

Subject Areas: Biology and Bio-materials

Facility: ESRF

Added On: 13/05/2010 11:17

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