Crystallization and Preliminary X-ray Diffraction Analysis of Hemextin A: a Unique Anticoagulant Protein from Hemachatus Haemachatus Venom

Overview

Journal Acta Crystallogr Sect F Struct Biol Cryst Commun

Date 2007 Aug 3

PMID 17671372

Citations 1

Authors

Yajnavalka Banerjee

Sundramurthy Kumar

Chacko Jobichen

R Manjunatha Kini

Affiliations

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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 P2(1)2(1)2(1), with unit-cell parameters a = 49.27, b = 49.51, c = 57.87 A and two molecules in the asymmetric unit. They diffracted to 1.5 A resolution at beamline X25 at BNL.

Citing Articles

In Silico Design of Novel Anticoagulant Peptides targeting Blood Coagulation Factor VIIa.

Al-Amri M, Alrasadi K, Bayoumi R, Banerjee Y Sultan Qaboos Univ Med J. 2011; 11(1):83-94.

PMID: 21509213 PMC: 3074690.

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