D J Johnson, P G Nugent, E G Tuddenham, K Harlos, G Kemball-Cook
Haemostasis Research Group, MRC Clinical Sciences Centre, Imperial College School of Medicine, Du Cane Road, London, W12 0NN, United Kingdom.
Journal of structural biology 1999 MarHuman coagulation factor VIIai that lacks the Gla domain (residues 1-44) has been prepared, purified, and crystallised. First, recombinant factor VII was activated to form factor VIIa, the active site was then inhibited with 1,5-dansyl-Glu-Gly-Arg-chloromethyl ketone, and finally the Gla domain was removed by chymotryptic digestion, yielding factor VIIai (des-Gla). After further purification single crystals suitable for x-ray analysis were obtained by vapour diffusion. Crystals of factor VIIai (des-Gla) belong to the tetragonal space group P41212 or P43212 with unit cell dimensions a = b = 94.85 A, c = 114.30 A, contain one molecule per asymmetric unit, and diffract to 2.3-A resolution when exposed to synchrotron radiation. Copyright 1999 Academic Press.
D J Johnson, P G Nugent, E G Tuddenham, K Harlos, G Kemball-Cook. Crystallization and preliminary X-ray analysis of active site-inhibited human coagulation factor VIIa (des-Gla). Journal of structural biology. 1999 Mar;125(1):90-3
PMID: 10196120
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