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

被引：0

作者：

Boyko, K. M. ^{[1
,2
]}

Nikolaeva, A. Yu. ^{[1
,2
]}

Kachalova, G. S. ^{[2
]}

Bonchuk, A. N. ^{[3
]}

Dorovatovskii, P. V. ^{[2
]}

Popov, V. O. ^{[1
,2
]}

机构：

[1] Russian Acad Sci, Fed Res Ctr Fundamentals Biotechnol, Moscow 119071, Russia

[2] Natl Res Ctr, Kurchatov Inst, Moscow 123098, Russia

[3] Russian Acad Sci, Inst Gene Biol, Moscow 119334, Russia

来源：

CRYSTALLOGRAPHY REPORTS | 2017年 / 62卷 / 06期

关键词：

CRYSTAL-STRUCTURE; INTERFACE; GENOME;

D O I：

10.1134/S1063774517060062

中图分类号：

O7 [晶体学];

学科分类号：

0702 ; 070205 ; 0703 ; 080501 ;

摘要：

The Drosophila genome has several dozens of transcription factors (TTK group) containing D'D cent D' 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 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.

引用

页码：912 / 915

页数：4

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