Abstract
Single crystals of the outer surface protein C (OspC) from Borrelia burgdorferi HB19 have been obtained by the vapor-diffusion method. These crystals belong to space group P2(1), with unit-cell parameters a = 66.218, b = 46.113, c = 112.079 A, beta = 99.30 degrees, and diffract to at least 2.2 A resolution. Native data have been collected from flash-frozen crystals at the National Synchrotron facility of Brookhaven National Laboratory. There are two dimers per asymmetric unit, related by a non-crystallographic twofold axis and a pseudo-translational symmetry.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Antigens, Bacterial*
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Bacterial Outer Membrane Proteins / chemistry*
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Bacterial Outer Membrane Proteins / genetics
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Bacterial Outer Membrane Proteins / isolation & purification
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Borrelia burgdorferi Group / genetics*
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray
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Escherichia coli / genetics
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Molecular Sequence Data
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Antigens, Bacterial
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Bacterial Outer Membrane Proteins
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OspC protein
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Recombinant Proteins