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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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.

作者简介

K. Boyko

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

编辑信件的主要联系方式.
Email: kmb@inbi.ras.ru
俄罗斯联邦, Moscow, 119071; Moscow, 123098

A. Nikolaeva

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

Email: kmb@inbi.ras.ru
俄罗斯联邦, Moscow, 119071; Moscow, 123098

G. Kachalova

National Research Centre “Kurchatov Institute,”

Email: kmb@inbi.ras.ru
俄罗斯联邦, Moscow, 123098

A. Bonchuk

Institute of Gene Biology

Email: kmb@inbi.ras.ru
俄罗斯联邦, Moscow, 119334

V. Popov

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

Email: kmb@inbi.ras.ru
俄罗斯联邦, Moscow, 119071; Moscow, 123098

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