Abstract
Human 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 groupP41212 orP43212 with unit cell dimensionsa=b= 94.85 Å,c= 114.30 Å, contain one molecule per asymmetric unit, and diffract to 2.3-Å resolution when exposed to synchrotron radiation.
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