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

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 domai...

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Published inCrystallography reports Vol. 62; no. 6; pp. 912 - 915
Main Authors Boyko, K. M., Nikolaeva, A. Yu, Kachalova, G. S., Bonchuk, A. N., Dorovatovskii, P. V., Popov, V. O.
Format Journal Article
LanguageEnglish
Published Moscow Pleiades Publishing 01.11.2017
Springer Nature B.V
Subjects
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
Crystallography and Scattering Methods
CRYSTALS
DIFFUSION
DROSOPHILA
Fruit flies
Insects
Physics
Physics and Astronomy
Proteins
RESOLUTION
SMALL ANGLE SCATTERING
Small angle X ray scattering
Structure of Macromolecular Compounds
THREE-DIMENSIONAL LATTICES
TRANSCRIPTION FACTORS
VAPORS
X-RAY DIFFRACTION
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Summary: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.
ISSN:1063-7745
1562-689X
DOI:10.1134/S1063774517060062