Open AccessAbsolute configuration of the hydroxyfarnesylethyl group of haem A, determined by X‐ray structural analysis of bovine heart cytochrome c oxidase using methods applicable at 2.8 Å resolution
Author(s) -
Yamashita Eiki,
Aoyama Hiroshi,
Yao Min,
Muramoto Kazumasa,
ShinzawaItoh Kyoko,
Yoshikawa Shinya,
Tsukihara Tomitake
Publication year - 2005
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444905023358
Subject(s) - absolute configuration , angstrom , resolution (logic) , chemistry , crystallography , cytochrome c oxidase , group (periodic table) , stereochemistry , computer science , enzyme , organic chemistry , artificial intelligence , biochemistry
The absolute configuration of haem A, the prosthetic group of cytochrome c oxidase, was determined to be S by analysis of the bond angles surrounding the chiral centre of haem A after refinement with X‐PLOR starting from respective initial structures with R and S configurations under absolute configuration constraints at 1.8 Å resolution. The same result was obtained by refinement at 1.8 Å resolution without the absolute configuration constraints. Both of these methods were applicable down to a resolution of about 2.8 Å. The constrained refinement converges more quickly than the unconstrained refinement.