Crystallization, data collection and processing of the chymotrypsin-BTCI-trypsin ternary complex.

Acta Crystallogr Sect F Struct Biol Cryst Commun 2007 Dec 30;63(Pt 12):1087-90. Epub 2007 Nov 30.

Laboratório de Biofísica, Instituto de Ciências Biológicas, Universidade de Brasília, 70910-900 Brasília-DF, Brazil.

A ternary complex of the black-eyed pea trypsin and chymotrypsin inhibitor (BTCI) with trypsin and chymotrypsin was crystallized by the sitting-drop vapour-diffusion method with 0.1 M HEPES pH 7.5, 10%(w/v) polyethylene glycol 6000 and 5%(v/v) 2-methyl-2,4-pentanediol as precipitant. BTCI is a small protein with 83 amino-acid residues isolated from Vigna unguiculata seeds and is able to inhibit trypsin and chymotrypsin simultaneously by forming a stable ternary complex. X-ray data were collected from a single crystal of the trypsin-BTCI-chymotrypsin ternary complex to 2.7 A resolution under cryogenic conditions. The structure of the ternary complex was solved by molecular replacement using the crystal structures of the BTCI-trypsin binary complex (PDB code 2g81) and chymotrypsin (PDB code 4cha) as search models.

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Source
http://dx.doi.org/10.1107/S1744309107056424DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2344091PMC
December 2007
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