title: Crystallization and preliminary crystallographic data of the PAS domain of the NifL protein from Azotobacter vinelandii.
abstract: The Azotobacter vinelandii NifL protein is a redox-sensing flavoprotein which inhibits the activity of the nitrogen-specific transcriptional activator NifA. The N-terminal PAS domain has been overexpressed in Escherichia coli and crystallized by the hanging-drop vapour-diffusion method. The crystal belongs to the rhombohedral space group R32, with unit-cell parameters a = b = 65.0, c = 157.3 A, and has one molecule in the asymmetric unit. Native data were collected to 3.0 A on the BW7B synchrotron beamline at the EMBL Hamburg Outstation.
authors.affiliation: Biochemistry, Dreyenlaan 3, 6703 HA Wageningen, The Netherlands.
authors.forename: M
authors.initials: M
authors.lastname: Hefti
authors.forename: J
authors.initials: J
authors.lastname: Hendle
authors.forename: C
authors.initials: C
authors.lastname: Enroth
authors.forename: J
authors.initials: J
authors.lastname: Vervoort
authors.forename: P A
authors.initials: PA
authors.lastname: Tucker
mesh_terms: D016948:Azotobacter vinelandii / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D013058:Mass Spectrometry; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D010446:Peptide Fragments; D011994:Recombinant Proteins; C084296:nifL protein, Bacteria