Abstract
The crystallization and structural characterization of bovine liver catalase (BLC) has been intensively studied for decades. Forms I and II of BLC have previously been fully characterized using single-crystal X-ray diffraction. Form III has previously been analyzed by electron microscopy, but owing to the thinness of this crystal form an X-ray crystal structure had not been determined. Here, the crystal structure of form III of BLC is presented in space group P2 12 12 1, with unit-cell parameters a = 68.7, b = 173.7, c = 186.3 Å. The asymmetric unit is composed of the biological tetramer, which is packed in a tetrahedron motif with three other BLC tetramers. This higher resolution structure has allowed an assessment of the previously published electron-microscopy studies. © 2011 International Union of Crystallography Printed in Singapore - all rights reserved.
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Foroughi, L. M., Kang, Y. N., & Matzger, A. J. (2011). Sixty years from discovery to solution: Crystal structure of bovine liver catalase form III. Acta Crystallographica Section D: Biological Crystallography, 67(9), 756–762. https://doi.org/10.1107/S0907444911024486
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