Purification, isolation, crystallization, and preliminary X-ray diffraction study of the BTB domain of the centrosomal protein 190 from Drosophila melanogaster


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Abstract

The spatial organization of the genome is controlled by a special class of architectural proteins, including proteins containing BTB domains that are able to dimerize or multimerize. The centrosomal protein 190 is one of such architectural proteins. The purification, crystallization, and preliminary X-ray diffraction study of the BTB domain of the centrosomal protein 190 are reported. The crystallization conditions were found by the vapor-diffusion technique. The crystals diffracted to 1.5 Å resolution and belonged to sp. gr. P3221. The structure was solved by the molecular replacement method. The structure refinement is currently underway.

About the authors

K. M. Boyko

Federal Research Centre “Fundamentals of Biotechnology,”; National Research Centre “Kurchatov Institute,”

Author for correspondence.
Email: kmb@inbi.ras.ru
Russian Federation, Moscow, 119071; Moscow, 123098

A. Yu. Nikolaeva

Federal Research Centre “Fundamentals of Biotechnology,”; National Research Centre “Kurchatov Institute,”

Email: kmb@inbi.ras.ru
Russian Federation, Moscow, 119071; Moscow, 123098

G. S. Kachalova

National Research Centre “Kurchatov Institute,”

Email: kmb@inbi.ras.ru
Russian Federation, Moscow, 123098

A. N. Bonchuk

Institute of Gene Biology

Email: kmb@inbi.ras.ru
Russian Federation, Moscow, 119334

V. O. Popov

Federal Research Centre “Fundamentals of Biotechnology,”; National Research Centre “Kurchatov Institute,”

Email: kmb@inbi.ras.ru
Russian Federation, Moscow, 119071; Moscow, 123098

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