title: X-ray crystallographic characterization and phasing of an NtrC homologue.
abstract: The ZraR (HydG) protein is a 441-amino-acid protein with three functional domains and is homologous to the general nitrogen-regulatory protein NtrC that regulates nitrogen assimilation in many bacteria. The AAA and DNA-binding domains (residues 141-441) of the ZraR protein from Salmonella typhimurium were crystallized using the sitting-drop vapour-diffusion method. X-ray diffraction data from the native crystal have been collected to 3.0 A resolution. Initial phasing was successfully performed by the SIRAS method using derivativatized crystals soaked in 1 mM ethylmercuric phosphate. Preliminary structural analysis shows the presence of a hexamer in the asymmetric unit. Model building is in progress.
authors.affiliation: European Molecular Biology Laboratory Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: László
authors.initials: L
authors.lastname: Sallai
authors.forename: Jörg
authors.initials: J
authors.lastname: Hendle
authors.forename: Paul A
authors.initials: PA
authors.lastname: Tucker
mesh_terms: D003001:Cloning, Molecular / Q000379:methods; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D012486:Salmonella typhimurium / Q000737:chemistry; D012645:Selenomethionine
chemical_list: D012645:Selenomethionine