Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 70, Issue -, Pages 1631-1635Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X14023188
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Funding
- Flanders Institute of Biotechnology (VIB) [PRJ9]
- Odysseus program of the Flanders Science Foundation (FWO)
- Hercules Foundation [UABR/09/005]
- Erasmus Mundus PhD fellowship
- Vetenskapsradet/VR
- Cancerfonden
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Helicobacter pylori is a human pathogen that colonizes about 50% of the world's population, causing chronic gastritis, duodenal ulcers and even gastric cancer. A steady emergence of multiple antibiotic resistant strains poses an important public health threat and there is an urgent requirement for alternative therapeutics. The blood group antigen-binding adhesin BabA mediates the intimate attachment to the host mucosa and forms a major candidate for novel vaccine and drug development. Here, the recombinant expression and crystallization of a soluble BabA truncation (BabA(25-460)) corresponding to the predicted extracellular adhesin domain of the protein are reported. X-ray diffraction data for nanobody-stabilized BabA 25-460 were collected to 2.25 angstrom resolution from a crystal that belonged to space group P2(1), with unit-cell parameters a = 50.96, b = 131.41, c = 123.40 angstrom, alpha = 90.0, beta = 94.8, gamma = 90.0 degrees, and which was predicted to contain two BabA(25-460)-nanobody complexes per asymmetric unit.
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