This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1aac
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1aac" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aac, resolution 1.31Å" /> '''AMICYANIN OXIDIZED, ...)
Next diff →
Revision as of 08:35, 20 November 2007
|
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
