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

Balasundaram Padmanabhan, Maria Scharlock, Kit I. Tong, Yoshihiro Nakamura, Moon Il Kang, Akira Kobayashi, Takehisa Matsumoto, Akiko Tanaka, Masayuki Yamamoto, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

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 P61 or P65, with unit-cell parameters a = b = 102.95, c = 55.21 Å, and contains one molecule in the asymmetric unit. A complete diffraction data was collected to 2.25 Å resolution using an R-AXIS IV++ imaging plate mounted on an RA-Micro7 Cu 14;Kα rotating-anode X-ray generator.

Original languageEnglish
Pages (from-to)153-155
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number1
DOIs
Publication statusPublished - 2005
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Fingerprint Dive into the research topics of 'Purification, crystallization and preliminary X-ray diffraction analysis of the Kelch-like motif region of mouse Keap1'. Together they form a unique fingerprint.

Cite this