Open AccessStructure at 1.6 Å resolution of the protein from gene locus At3g22680 from Arabidopsis thaliana
Author(s) -
Allard Simon T. M.,
Bingman Craig A.,
Johnson Kenneth A.,
Bitto Eduard,
Jeon Won Bae,
Wesenberg Gary E.,
Phillips George N.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105019743
Subject(s) - chaps , arabidopsis , arabidopsis thaliana , locus (genetics) , gene product , homology (biology) , gene , resolution (logic) , monomer , chemistry , crystallography , protein structure , stereochemistry , biology , mutant , biochemistry , gene expression , enzyme , organic chemistry , artificial intelligence , computer science , polymer
The gene product of At3g22680 from Arabidopsis thaliana codes for a protein of unknown function. The crystal structure of the At3g22680 gene product was determined by multiple‐wavelength anomalous diffraction and refined to an R factor of 16.0% ( R free = 18.4%) at 1.60 Å resolution. The refined structure shows one monomer in the asymmetric unit, with one molecule of the non‐denaturing detergent CHAPS {3‐[(3‐cholamidopropyl)dimethylammonio]‐1‐propane sulfonate} tightly bound. Protein At3g22680 shows no structural homology to any other known proteins and represents a new fold in protein conformation space.