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

doi:10.1107/S1744309104032506

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

Tohoku Medical Megabank Organization (ToMMo)

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15 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 language	English
Pages (from-to)	153-155
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	61
Issue number	1
DOIs	https://doi.org/10.1107/S1744309104032506
Publication status	Published - 2005

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Padmanabhan, B., Scharlock, M., Tong, K. I., Nakamura, Y., Kang, M. I., Kobayashi, A., Matsumoto, T., Tanaka, A., Yamamoto, M., & Yokoyama, S. (2005). 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, 61(1), 153-155. https://doi.org/10.1107/S1744309104032506

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

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 {\AA}, and contains one molecule in the asymmetric unit. A complete diffraction data was collected to 2.25 {\AA} resolution using an R-AXIS IV++ imaging plate mounted on an RA-Micro7 Cu 14;Kα rotating-anode X-ray generator.",

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

year = "2005",

doi = "10.1107/S1744309104032506",

language = "English",

volume = "61",

pages = "153--155",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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Padmanabhan, B, Scharlock, M, Tong, KI, Nakamura, Y, Kang, MI, Kobayashi, A, Matsumoto, T, Tanaka, A, Yamamoto, M & Yokoyama, S 2005, '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, vol. 61, no. 1, pp. 153-155. https://doi.org/10.1107/S1744309104032506

Purification, crystallization and preliminary X-ray diffraction analysis of the Kelch-like motif region of mouse Keap1. / Padmanabhan, Balasundaram; Scharlock, Maria; Tong, Kit I. et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 61, No. 1, 2005, p. 153-155.

Research output: Contribution to journal › Article › peer-review

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AU - Padmanabhan, Balasundaram

AU - Scharlock, Maria

AU - Tong, Kit I.

AU - Nakamura, Yoshihiro

AU - Kang, Moon Il

AU - Kobayashi, Akira

AU - Matsumoto, Takehisa

AU - Tanaka, Akiko

AU - Yamamoto, Masayuki

AU - Yokoyama, Shigeyuki

PY - 2005

Y1 - 2005

N2 - 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.

AB - 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.

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

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