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

Publisher： John Wiley & Sons Inc

E-ISSN： 1744-3091|63|8|701-703

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.63, Iss.8, 2007-08, pp. : 701-703

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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.