Purification, crystallization, and preliminary X-ray characterization of a 36 kDa amaranth globulin.
The purpose of this study was to purify, crystallize, and characterize by X-ray diffraction an amaranth globulin for its subsequent structure elucidation. A 36-kDa amaranth globulin was extracted by sequential precipitation and purified by gel filtration and cationic exchange columns. It was crystallized at 18 degrees C from 4 M sodium formate. Suitable crystals for X-ray analysis were found to belong to the tetragonal crystal system with cell dimensions of a = b = 195.5 A and c = 164.14 A. Two possible tetragonal space groups P4(1)2(1)2 or P4(3)2(1)2 were determined. The crystals diffracted up to 2.5 A.
Vasco-Méndez
N L
NL
Departamento de Biotecnología y Bioingeniería, Centro de Investigación y de Estudios Avanzados del IPN, Unidad Zacatenco, Avenida Instituto Politécnico Nacional 2508, Col. San Pedro Zacatenco, 07360 Mexico, D.F., Departamento de.
Soriano-García
M
M
Moreno
A
A
Castellanos-Molina
R
R
Paredes-López
O
O
D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003460:Crystallization; D018360:Crystallography, X-Ray; D005916:Globulins / Q000737:chemistry* / Q000302:isolation & purification; D010945:Plants, Edible / Q000737:chemistry; D012639:Seeds / Q000737:chemistry*
D005916:Globulins