1aac
From Proteopedia
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AMICYANIN OXIDIZED, 1.31 ANGSTROMS
Overview
High-resolution X-ray diffraction data to d(min) = 1.31 A were collected, on a Xuong-Hamlin area detector from crystals of the blue-copper protein, amicyanin, isolated from P. denitrificans. With coordinates from the, earlier 2.0 A structure determination as a starting point, simulated, annealing and restrained positional and temperature factor refinements, using the program X-PLOR resulted in a final R factor of 15.5%, based on, 21 131 unique reflections in the range 8.0-1.3 A. Comparison of the 1.31 A, structure with that at 2.0 A shows the same basic features. However, the, high-resolution electron-density maps clearly reveal additional solvent, molecules and significant discrete disorder in protein side chains and, within the solvent structure. As a consequence of modelling side-chain, disorder, several new hydrogen-bonding interactions were identified.
About this Structure
1AAC is a Single protein structure of sequence from Paracoccus denitrificans with CU as ligand. Full crystallographic information is available from OCA.
Reference
X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31 A resolution., Cunane LM, Chen ZW, Durley RC, Mathews FS, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):676-86. PMID:15299631
Page seeded by OCA on Tue Nov 20 10:42:57 2007
