Literature DB >> 16511174

Crystallization and preliminary X-ray diffraction analysis of a new chitin-binding protein from Parkia platycephala seeds.

Benildo S Cavada1, Rolando E R Castellón, Georg G Vasconcelos, Bruno A M Rocha, Gustavo A Bezerra, Henri Debray, Plínio Delatorre, Celso S Nagano, Marcos Toyama, Vicente P T Pinto, Frederico B M B Moreno, Fernanda Canduri, Walter F de Azevedo.   

Abstract

A chitin-binding protein named PPL-2 was purified from Parkia platycephala seeds and crystallized. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 55.19, b = 59.95, c = 76.60 A, 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 A 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.

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Year:  2005        PMID: 16511174      PMCID: PMC1978108          DOI: 10.1107/S1744309105024462

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  16 in total

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3.  Basic local alignment search tool.

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Authors:  B W Matthews
Journal:  J Mol Biol       Date:  1968-04-28       Impact factor: 5.469

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Authors:  A C Terwisscha van Scheltinga; M Hennig; B W Dijkstra
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10.  Heavy-metal-responsive genes in maize: identification and comparison of their expression upon various forms of abiotic stress.

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  1 in total

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