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- Title
Crystallization and X-ray diffraction analysis of the CH domain of the cotton kinesin GhKCH2.
- Authors
Chen, Ziwei; Li, Ping; Liu, Guoqin; Qin, Xinghua
- Abstract
GhKCH2 belongs to a group of plant-specific kinesins (KCHs) containing an actin-binding calponin homology (CH) domain in the N-terminus. Previous studies revealed that the GhKCH2 CH domain (GhKCH2-CH) had a higher affinity for F-actin ( Kd = 0.42 ± 0.02 µ M) than most other CH-domain-containing proteins. To understand the underlying mechanism, prokaryotically expressed GhKCH2-CH (amino acids 30-166) was purified and crystallized. Crystals were grown by the sitting-drop vapour-diffusion method using 0.1 M Tris-HCl pH 7.0, 20%( w/ v) PEG 8000 as a precipitant. The crystals diffracted to a resolution of 2.5 Å and belonged to space group P21, with unit-cell parameters a = 41.57, b = 81.92, c = 83.00 Å, α = 90.00, β = 97.31, γ = 90.00°. Four molecules were found in the asymmetric unit with a Matthews coefficient of 2.22 Å3 Da−1, corresponding to a solvent content of 44.8%.
- Subjects
KINESIN; CALPONIN; X-ray diffraction
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2016, Vol 72, Issue 3, p240
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X16001825