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Updated: Aug 11, 2026

Purification of the M. magneticum Strain AMB-1 Magnetosome Associated Protein MamAΔ41
Published on: March 25, 2010
Purification, crystallization, and preliminary X-ray characterization of a 36 kDa amaranth globulin
N L Vasco-Méndez1, M Soriano-García, A Moreno
1Departamento 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.
Abstract:
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.

