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

被引:6
作者
Cavada, BS
Castellón, RER
Vasconcelos, GG
Rocha, BAM
Bezerra, GA
Debray, H
Delatorre, P
Nagano, CS
Toyama, M
Pinto, VPT
Moreno, FBMB
Canduri, F
de Azevedo, WF
机构
[1] Univ Fed Ceara, Dept Bioquim & Biol Mol, Biomol Lab, BR-60451970 Fortaleza, Ceara, Brazil
[2] Univ Sci & Tech Lille Flandres Artois, Chim Biol Lab, Villeneuve Dascq, France
[3] Univ Sci & Tech Lille Flandres Artois, CNRS, UMR 8576, Villeneuve Dascq, France
[4] Univ Reg Cariri, Dept Ciencias Biol, BR-63105000 Crato, Brazil
[5] Univ Estadual Campinas, UNICAMP, Inst Biol, Dept Bioquim, Campinas, SP, Brazil
[6] UNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2005年 / 61卷
关键词
D O I
10.1107/S1744309105024462
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom, 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 angstrom 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.
引用
收藏
页码:841 / 843
页数:3
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