ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
Two crystal forms of component 1 (the MoFe protein) of nitrogenase from Klebsiella pneumoniae have been isolated and characterized. The triclinic form has cell dimensions a = 76.0, b = 109.6, c = 144.6 Å, α = 80.3, β = 74.9 and γ = 69.6°, diffracts to around 3.0 Å and has two molecules in the asymmetric unit. The monoclinic form belongs to space group P21 with a = 76.6, b = 127.8, c = 109.1 Å and β = 104.6° (frozen at 100 K), diffracts to 1.5 Å and has one molecule in the asymmetric unit. At this resolution the outstanding questions concerning the structure and the operation of the enzyme, in particular the linkage between the Fe4S4 units in the P clusters, the true geometry of the apparently trigonal Fe atoms in the FeMoco and the reduction site itself, should be answerable.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444996012681
