Abstract
The Escherichia coli stress protein YciF was overexpressed and purified by three chromatographic steps. Crystals were obtained using ammonium sulfate as a precipitant. The YciF protein crystals diffracted beyond 2.25 A resolution using a rotating-anode X-ray source. The lattice type is rhombohedral, with unit-cell parameters a = b = 80.0, c = 131.03 A, alpha = beta = 90.0, gamma = 120.0 degrees. The crystal belongs to space group R32.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Crystallography, X-Ray
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Escherichia coli / metabolism*
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Escherichia coli Proteins / chemistry*
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Heat-Shock Proteins / chemistry*
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Molecular Sequence Data
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Protein Conformation
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Recombinant Proteins / chemistry
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Sequence Homology, Amino Acid
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X-Ray Diffraction
Substances
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Escherichia coli Proteins
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Heat-Shock Proteins
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Recombinant Proteins
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YciF protein, E coli