Crystallization of mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil

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Abstract

In adult Ascaris suum (roundworm) mitochondrial membrane-bound complex II acts as a rhodoquinol-fumarate reductase, which is the reverse reaction to that of mammalian complex II (succinate-ubiquinone reductase). The adult A. suum rhodoquinol-fumarate reductase was crystallized in the presence of octaethyleneglycol monododecyl ether and n-dodecyl-Β-d-maltopyranoside in a 3:2 weight ratio. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 123.75, b = 129.08, c = 221.12 Å, and diffracted to 2.8 Å resolution using synchrotron radiation. The presence of two molecules in the asymmetric unit (120 kDa 2) gives a crystal volume per protein mass (V M) of 3.6 Å3 Da-1. © 2009 International Union of Crystallography All rights reserved.

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Osanai, A., Harada, S., Sakamoto, K., Shimizu, H., Inaoka, D. K., & Kita, K. (2009). Crystallization of mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(9), 941–944. https://doi.org/10.1107/S1744309109031352

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