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The X-ray crystal structure of Klebsiella pneumoniae nitrogenase component 1
Reference
JRI07336
Principal Investigator / Supervisor
Professor David Lawson
Co-Investigators /
Co-Supervisors
Professor Andrew Hemmings
Institution
John Innes Centre
Department
Disease and Stress Biology
Funding type
Research
Value (£)
9,496
Status
Completed
Type
Research Grant
Start date
01/04/1997
End date
01/10/1997
Duration
6 months
Abstract
Nitrogenases play a central role in the fundamental process of biological nitrogen fixation. We have crystals of the component 1 of the enzyme isolated from Klebsiella pneumoniae which diffract X-rays to high resolution when flash-frozen. Through X-ray analysis we intend to determine the three-dimensional structure of this enzyme and characterise a number of interesting site-directed mutants.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
Joint Equipment Research Initiative 1996 (JE1) [1996]
Funding Scheme
X – not Funded via a specific Funding Scheme
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