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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Sep 1;61(Pt 9):841-3. Epub 2005 Aug 31.

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

Author information

1
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Biomol-Lab, CEP 60451-970, Caixa Postal 6043, Fortaleza-Ceará, Brazil. bscavada@ufc.br

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.

PMID:
16511174
PMCID:
PMC1978108
DOI:
10.1107/S1744309105024462
[Indexed for MEDLINE]
Free PMC Article

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