Crystallization and preliminary X-ray analysis of Borrelia burgdorferi outer surface protein C (OspC).
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.
Kumaran
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Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
Eswaramoorthy
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Dunn
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Swaminathan
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D000595:Amino Acid Sequence; D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D015748:Borrelia burgdorferi Group / Q000235:genetics*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; C079616:OspC protein; D011994:Recombinant Proteins