Crystallization and preliminary crystallographic data of the PAS domain ofthe NifL protein from Azotobacter vinelandii

Authors
Hefti, M Hendle, J Enroth, C Vervoort, J Tucker, PA
Citation
M. Hefti et al., Crystallization and preliminary crystallographic data of the PAS domain ofthe NifL protein from Azotobacter vinelandii, ACT CRYST D, 57, 2001, pp. 1895-1896
Citations number
24
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
12
Pages
1895 - 1896
Database
ISI
SICI code
0907-4449(200112)57:<1895:CAPCDO>2.0.ZU;2-9
Abstract
The Azotobacter vinelandii NifL protein is a redox-sensing flavoprotein whi ch 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 Angstrom, and has one molecule in the asymmetric unit. Native data were collected to 3.0 Angstrom on the BW7B synchrotron beamline at th e EMBL Hamburg Outstation.