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

M.H. Hefti, J. Hendle, C. Enroth, J.J.M. Vervoort, P.A. Tucker

Research output: Contribution to journalArticleAcademicpeer-review

6 Citations (Scopus)

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 Å, and has one molecule in the asymmetric unit. Native data were collected to 3.0 Å on the BW7B synchrotron beamline at the EMBL Hamburg Outstation.
Original languageEnglish
Pages (from-to)1895-1896
JournalActa Crystallographica Section D-Biological Crystallography
Volume57
Issue number12
DOIs
Publication statusPublished - 2001

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