Literature DB >> 11717509

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

M Hefti1, J Hendle, C Enroth, J Vervoort, P A Tucker.   

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.

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Year:  2001        PMID: 11717509     DOI: 10.1107/s0907444901015657

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

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  2 in total

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