Crystallization and preliminary X-ray diffraction analysis of a new chitin-binding protein from Parkia platycephala seeds
- Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Biomol-Lab, CEP 60451-970, Caixa Postal 6043, Fortaleza-Ceará (Brazil)
- Laboratoire de Chimie Biologique et Unité Mixte de Recherche du CNRS No. 8576, Université des Sciences et Technologies de Lille, Villeneuve d’Ascq (France)
- Departamento de Bioquímica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Campinas, SP (Brazil)
Crystals of P. platycephala chintinase/lectin (PPL-2) belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 55.19, b = 59.95, c = 76.60 Å. The preliminary cystal structure of PPL-2 was solved at a resolution of 1.73 Å by molecular replacement, presenting a correlation coefficient of 0.558 and an R factor of 0.439. A chitin-binding protein named PPL-2 was purified from Parkia platycephala seeds and crystallized. Crystals belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 55.19, b = 59.95, c = 76.60 Å, and grew over several days at 293 K using the hanging-drop method. Using synchrotron radiation, a complete structural data set was collected to 1.73 Å resolution. The preliminary crystal structure of PPL-2, determined by molecular replacement, presents a correlation coefficient of 0.558 and an R factor of 0.439. Crystallographic refinement is in progress.
- OSTI ID:
- 22356158
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 9; Other Information: PMCID: PMC1978108; PMID: 16511174; PUBLISHER-ID: vr5036; OAI: oai:pubmedcentral.nih.gov:1978108; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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