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

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.

SUBMITTER: Cavada BS

PROVIDER: S-EPMC1978108 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature

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

Cavada Benildo S BS Castellón Rolando E R RE Vasconcelos Georg G GG Rocha Bruno A M BA Bezerra Gustavo A GA Debray Henri H Delatorre Plínio P Nagano Celso S CS Toyama Marcos M Pinto Vicente P T VP Moreno Frederico B M B FB Canduri Fernanda F Azevedo Walter F de WF

Acta crystallographica. Section F, Structural biology and crystallization communications 20050831 Pt 9

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 coefficien ...[more]

PMID: 16511174

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