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Crystallization and preliminary X-ray analysis of Borrelia burgdorferi outer surface protein A (OspA) complexed with a murine monoclonal antibody Fab fragment.

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Abstract

The Borrelia burgdorferi outer surface lipoprotein OspA is a current focus for vaccine development to prevent
Lyme disease infection. A soluble, recombinant form of the protein lacking the amino-terminal lipid membrane anchor was cocrystallized with the Fab fragment of an agglutinating mouse monoclonal antibody. The crystals belong to space group P2(1)2(1)2(1), with a = 90.0 A, b = 91.9 A, and c = 102.9 A and they were found to diffract to a maximum resolution of 2.8 A using synchrotron radiation.

J Struct Biol. 1995 Nov-Dec;115(3):335-7. Research Support, Non-U.S. Gov’t; Research Support, U.S. Gov’t, Non-P.H.S.

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