Purification, crystallization and preliminary X-ray diffraction analysis of the Kelch-like motif region of mouse Keap1

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Balasundaram PadmanabhanShigeyuki Yokoyama

Abstract

Keap1 (Kelch-like ECH-associating protein 1) is a negative regulator of the Nrf2 transcription factor in the cytoplasm. The Kelch/DGR (double-glycine repeat) domain of Keap1 associates with Nrf2 as well as with actin filaments. A recombinant protein containing both the Kelch/DGR domain and the C-terminal region of mouse Keap1 was expressed in Escherichia coli, purified to near-homogeneity and crystallized by the sitting-drop vapour-diffusion method. The crystal belongs to space group P6(1) or P6(5), with unit-cell parameters a = b = 102.95, c = 55.21 A, and contains one molecule in the asymmetric unit. A complete diffraction data was collected to 2.25 A resolution using an R-AXIS IV++ imaging plate mounted on an RA-Micro7 Cu Kalpha rotating-anode X-ray generator.

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Citations

Apr 19, 2008·Journal of Synchrotron Radiation·Balasundaram PadmanabhanShigeyuki Yokoyama
Apr 9, 2008·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Balasundaram PadmanabhanShigeyuki Yokoyama
Mar 3, 2011·Archives of Toxicology·Liam Baird, Albena T Dinkova-Kostova
Mar 2, 2006·Molecular Cell·Balasundaram PadmanabhanMasayuki Yamamoto
Apr 3, 2020·Free Radical Biology & Medicine·Aleksandra KopaczAnna Grochot-Przeczek
May 30, 2006·The Journal of Experimental Biology·Chris GoldringB Kevin Park

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