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Title
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Crystallization, data collection and processing of the chymotrypsin-BTCI-trypsin ternary complex.
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Authors
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G.F.Esteves,
R.C.Teles,
N.S.Cavalcante,
D.Neves,
M.M.Ventura,
J.A.Barbosa,
S.M.de Freitas.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007,
63,
1087-1090.
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PubMed id
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Abstract
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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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