Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 395 - 397 |
| Number of pages | 3 |
| Journal | Acta Crystallographica. Section F: Structural Biology Communications |
| Volume | 65 |
| Issue number | Pt 4 |
| Publication status | Published - 2009 |
Cite this
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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 journal › Article › Research › peer-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
N2 - 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.
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
JF - Acta Crystallographica. Section F: Structural Biology Communications
SN - 2053-230X
IS - Pt 4
ER -