Crystallization and preliminary crystallographic studies of Schizolobium parahyba chymotrypsin inhibitor (SPCI) at 1.8 Å resolution
- Laboratório de Biofísica, Instituto de Ciências Biológicas, Universidade de Brasília, Brasília-DF, 70910-900 (Brazil)
- Laboratório de Espectrometria de Massa, Empresa Brasileira de Pesquisa Agropecuária - Recursos Genéticos e Biotecnologia, Brasília-DF, 70770-900 (Brazil)
Crystallization and preliminary crystallographic studies of Schizolobium parahyba chymotrypsin inhibitor (SPCI) at 1.8 Å resolution. SPCI, a Kunitz-type chymotrypsin inhibitor, is a 180-amino-acid polypeptide isolated from Schizolobium parahyba seeds. This inhibitor has been characterized as a highly stable protein over a broad pH and temperature range. SPCI was crystallized using a solution containing 0.1 M sodium acetate trihydrate buffer pH 4.6, 33%(v/v) PEG 2000 and 0.2 M ammonium sulfate. Data were collected to 1.80 Å resolution from a single crystal of SPCI under cryogenic conditions. The protein crystallized in space group P2{sub 1}2{sub 1}2, with unit-cell parameters a = 40.01, b = 71.58, c = 108.68 Å and an R{sub merge} of 0.052. The structure of SPCI has been solved by molecular replacement using the known structure of the Kunitz-type trypsin inhibitor from Delonix regia (PDB code) as the search model.
- OSTI ID:
- 22360421
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 11; Other Information: PMCID: PMC2339747; PMID: 18007042; PUBLISHER-ID: en5261; OAI: oai:pubmedcentral.nih.gov:2339747; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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