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Crystallization and preliminary X‐ray diffraction analysis of hemextin A: a unique anticoagulant protein from Hemachatus haemachatus venom

Crystallization and preliminary X‐ray diffraction analysis of hemextin A: a unique anticoagulant... Hemextin A was isolated and purified from African Ringhals cobra (Hemachatus haemachatus). It is a three‐finger toxin that specifically inhibits blood coagulation factor VIIa and clot formation and that also interacts with hemextin B to form a unique anticoagulant complex. Hemextin A was crystallized by the hanging‐drop vapour‐diffusion method by equilibration against 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate pH 4.6 and 30% PEG 4000 as the precipitating agent. The crystals belong to space group P212121, with unit‐cell parameters a = 49.27, b = 49.51, c = 57.87 Å and two molecules in the asymmetric unit. They diffracted to 1.5 Å resolution at beamline X25 at BNL. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary X‐ray diffraction analysis of hemextin A: a unique anticoagulant protein from Hemachatus haemachatus venom

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References (13)

Publisher
Wiley
Copyright
Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309107034239
pmid
17671372
Publisher site
See Article on Publisher Site

Abstract

Hemextin A was isolated and purified from African Ringhals cobra (Hemachatus haemachatus). It is a three‐finger toxin that specifically inhibits blood coagulation factor VIIa and clot formation and that also interacts with hemextin B to form a unique anticoagulant complex. Hemextin A was crystallized by the hanging‐drop vapour‐diffusion method by equilibration against 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate pH 4.6 and 30% PEG 4000 as the precipitating agent. The crystals belong to space group P212121, with unit‐cell parameters a = 49.27, b = 49.51, c = 57.87 Å and two molecules in the asymmetric unit. They diffracted to 1.5 Å resolution at beamline X25 at BNL.

Journal

Acta Crystallographica Section FWiley

Published: Aug 1, 2007

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