Crystallization and preliminary X-ray diffraction analysis of a new chitin-binding protein from Parkia platycephala seeds.
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.
Cavada
Benildo S
BS
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Biomol-Lab, CEP 60451-970, Caixa Postal 6043, Fortaleza-Ceará, Brazil. bscavada@ufc.br
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
D000595:Amino Acid Sequence; D002686:Chitin / Q000378:metabolism*; D003460:Crystallization; D007887:Fabaceae / Q000737:chemistry*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D011485:Protein Binding; D012639:Seeds / Q000737:chemistry*; D016415:Sequence Alignment; D014961:X-Ray Diffraction
D010940:Plant Proteins; D002686:Chitin