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

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

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 aminoterminal lipid membrane anchor was cocrystallized with the Fab fragment of an agglutinating mouse monoclonal antibody. The crystals belong to space group P212121 with a = 90.0 Å, b = 91.9 Å, and c = 102.9 Å and they were found to diffract to a maximum resolution of 2.8 Å using synchrotron radiation.

Original languageEnglish (US)
Pages (from-to)335-337
Number of pages3
JournalJournal of Structural Biology
Volume115
Issue number3
DOIs
StatePublished - Nov 1995
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology

Fingerprint

Dive into the research topics of 'Crystallization and preliminary X-ray analysis of Borrelia burgdorferi outer surface protein a (OspA) complexed with a murine monoclonal antibody fab fragment'. Together they form a unique fingerprint.

Cite this