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. 2007 Aug 1;63(Pt 8):701-3.
doi: 10.1107/S1744309107034239. Epub 2007 Jul 21.

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

Yajnavalka Banerjee  1 , Sundramurthy Kumar, Chacko Jobichen, R Manjunatha Kini
Affiliations

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

Yajnavalka Banerjee et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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.

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Figures

Figure 1
Figure 1
(a) Size-exclusion chromatography elution profile of hemextin A. (b) Molecular-weight standards. (c) Mass spectrum of hemextin A.
Figure 2
Figure 2
Crystal of hemextin A. Ten divisions of the scale is equivalent to 0.17 mm.
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References

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