Crystallization and preliminary X-ray analysis of a rat aldose reductase-like protein (AKR1B14)

Roland Poh-Tuck Chung, Satoshi Endo, Akira Hara, Ossama El-Kabbani

Research output: Contribution to journalArticleResearchpeer-review

3 Citations (Scopus)

Abstract

Mouse vas deferens protein/aldo- keto reductase 1B7 (AKR1B7) is involved in the detoxification of isocaproaldehyde, a steroidogenesis byproduct, and of 4-hydroxynonenal formed by lipid peroxidation. The rat orthologue of AKR1B7 has recently been named AKR1B14 in the AKR superfamily. Recombinant AKR1B14 was expressed in a bacterial system and purified to homogeneity. The purified protein was crystallized from polyethylene glycol solutions using the hanging-drop vapour-diffusion method and an X-ray diffraction data set was collected to 1.86 angstrom resolution. The crystals belonged to space group P2(1), with unit-cell parameters a = 50.66, b = 69.14, c = 72.27 angstrom, beta = 96.4 degrees. This is the first crystallization report of a rodent AKR1B7 orthologue.
Original languageEnglish
Pages (from-to)395 - 397
Number of pages3
JournalActa Crystallographica. Section F: Structural Biology Communications
Volume65
Issue numberPt 4
Publication statusPublished - 2009

Cite this

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title = "Crystallization and preliminary X-ray analysis of a rat aldose reductase-like protein (AKR1B14)",
abstract = "Mouse vas deferens protein/aldo- keto reductase 1B7 (AKR1B7) is involved in the detoxification of isocaproaldehyde, a steroidogenesis byproduct, and of 4-hydroxynonenal formed by lipid peroxidation. The rat orthologue of AKR1B7 has recently been named AKR1B14 in the AKR superfamily. Recombinant AKR1B14 was expressed in a bacterial system and purified to homogeneity. The purified protein was crystallized from polyethylene glycol solutions using the hanging-drop vapour-diffusion method and an X-ray diffraction data set was collected to 1.86 angstrom resolution. The crystals belonged to space group P2(1), with unit-cell parameters a = 50.66, b = 69.14, c = 72.27 angstrom, beta = 96.4 degrees. This is the first crystallization report of a rodent AKR1B7 orthologue.",
author = "Chung, {Roland Poh-Tuck} and Satoshi Endo and Akira Hara and Ossama El-Kabbani",
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Crystallization and preliminary X-ray analysis of a rat aldose reductase-like protein (AKR1B14). / Chung, Roland Poh-Tuck; Endo, Satoshi; Hara, Akira; El-Kabbani, Ossama.

In: Acta Crystallographica. Section F: Structural Biology Communications, Vol. 65, No. Pt 4, 2009, p. 395 - 397.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Crystallization and preliminary X-ray analysis of a rat aldose reductase-like protein (AKR1B14)

AU - Chung, Roland Poh-Tuck

AU - Endo, Satoshi

AU - Hara, Akira

AU - El-Kabbani, Ossama

PY - 2009

Y1 - 2009

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AB - Mouse vas deferens protein/aldo- keto reductase 1B7 (AKR1B7) is involved in the detoxification of isocaproaldehyde, a steroidogenesis byproduct, and of 4-hydroxynonenal formed by lipid peroxidation. The rat orthologue of AKR1B7 has recently been named AKR1B14 in the AKR superfamily. Recombinant AKR1B14 was expressed in a bacterial system and purified to homogeneity. The purified protein was crystallized from polyethylene glycol solutions using the hanging-drop vapour-diffusion method and an X-ray diffraction data set was collected to 1.86 angstrom resolution. The crystals belonged to space group P2(1), with unit-cell parameters a = 50.66, b = 69.14, c = 72.27 angstrom, beta = 96.4 degrees. This is the first crystallization report of a rodent AKR1B7 orthologue.

UR - http://scripts.iucr.org/cgi-bin/paper?S1744309109009762

M3 - Article

VL - 65

SP - 395

EP - 397

JO - Acta Crystallographica. Section F: Structural Biology Communications

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SN - 2053-230X

IS - Pt 4

ER -