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|Title:||Crystallization and preliminary X-ray analysis of a novel Kunitz-type kallikrein inhibitor from Bauhinia bauhinioides|
Vierira, D. F.
Araujo, APU de
Garratt, R. C.
Universidade de São Paulo (USP)
Universidade Federal de Minas Gerais (UFMG)
Universidade Federal de São Paulo (UNIFESP)
|Citation:||Acta Crystallographica Section F-structural Biology and Crystallization Communications. Malden: Wiley-Blackwell, v. 61, p. 910-913, 2005.|
|Abstract:||A Kunitz-type protease inhibitor (BbKI) found in Bauhinia bauhinioides seeds has been overexpressed in Escherichia coli and crystallized at 293 K using PEG 4000 as the precipitant. X-ray diffraction data have been collected to 1.87 A resolution using an in-house X-ray generator. the crystals of the recombinant protein (rBbKI) belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 46.70, b = 64.14, c = 59.24 angstrom. Calculation of the Matthews coefficient suggests the presence of one monomer of rBbKI in the asymmetric unit, with a corresponding solvent content of 51% (V(M) = 2.5 angstrom(3) Da(-1)). Iodinated crystals were prepared and a derivative data set was also collected at 2.1 angstrom resolution. Crystals soaked for a few seconds in a cryogenic solution containing 0.5 M NaI were found to be reasonably isomorphous to the native crystals. Furthermore, the presence of iodide anions could be confirmed in the NaI-derivatized crystal. Data sets from native and derivative crystals are being evaluated for use in crystal structure determination by means of the SIRAS (single isomorphous replacement with anomalous scattering) method.|
|Appears in Collections:||Em verificação - Geral|
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