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PDBsum entry 1e9m
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Iron-sulfur protein
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PDB id
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1e9m
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystallization and preliminary X-Ray diffraction analysis of a [2fe-2s] ferredoxin (fdvi) from rhodobacter capsulatus.
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Authors
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J.Armengaud,
G.Sainz,
Y.Jouanneau,
L.C.Sieker.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2001,
57,
301-303.
[DOI no: ]
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PubMed id
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Abstract
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ferredoxin found in the photosynthetic bacterium Rhodobacter
capsulatus has been purified in recombinant form from Escherichia coli. This
protein, called FdVI, resembles ferredoxins involved in iron-sulfur cluster
biosynthesis in various prokaryotic and eukaryotic cells. Purified recombinant
FdVI was recovered in high yields and appeared to be indistinguishable from the
genuine R. capsulatus ferredoxin based on UV-visible absorption and EPR
spectroscopy and mass spectrometry. FdVI has been crystallized in the oxidized
state by a sitting-drop vapour-diffusion technique using sodium formate as
precipitant. Seeding larger drops from a previous hanging-drop-grown small
crystal resulted in the formation of long red-brown prismatic needles.
Preliminary X-ray diffraction analysis indicated that FdVI crystals are
orthorhombic and belong to the space group P2(1)2(1)2(1), with unit-cell
parameters a = 45.87, b = 49.83, c = 54.29 A.
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Figure 2.
Figure 2 Recombinant FdVI crystals.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2001,
57,
301-303)
copyright 2001.
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