Preliminary small-angle X-ray scattering and X-ray diffraction studies of the BTB domain of lola protein from Drosophila melanogaster


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The Drosophila genome has several dozens of transcription factors (TTK group) containing ВТВ domains assembled into octamers. The LOLA protein belongs to this family. The purification, crystallization, and preliminary X-ray diffraction and small-angle X-ray scattering (SAXS) studies of the BTB domain of this protein are reported. The crystallization conditions were found by the vapor-diffusion technique. A very low diffraction resolution (8.7 Å resolution) of the crystals was insufficient for the determination of the threedimensional structure of the BTB domain. The SAXS study demonstrated that the BTB domain of the LOLA protein exists as an octamer in solution.

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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

P. Dorovatovskii

National Research Centre “Kurchatov Institute,”

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

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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