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

被引：5

作者：

Hefti, M ^{[1
]}

Hendle, J ^{[1
]}

Enroth, C ^{[1
]}

Vervoort, J ^{[1
]}

Tucker, PA ^{[1
]}

机构：

[1] DESY, EMBL, Hamburg Outstn, D-22603 Hamburg, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444901015657

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom, and has one molecule in the asymmetric unit. Native data were collected to 3.0 Angstrom on the BW7B synchrotron beamline at the EMBL Hamburg Outstation.

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页码：1895 / 1896

页数：2

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