Structure at 1.6 Å resolution of the protein from gene locus At3g22680 from Arabidopsis thaliana

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% (Rfree = 18.4%) at 1.60 Å resolution. The refined struc...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-07, Vol.61 (7), p.647-650
Main Authors: Allard, Simon T. M., Bingman, Craig A., Johnson, Kenneth A., Bitto, Eduard, Jeon, Won Bae, Wesenberg, Gary E., Phillips Jr, George N.
Format: Article
Language:English
Subjects:
Arabidopsis - metabolism
Arabidopsis thaliana
At3g22680
Cholic Acids - pharmacology
Cloning, Molecular
Crystallization
Crystallography, X-Ray - methods
Detergents - pharmacology
Electrophoresis, Polyacrylamide Gel
Models, Statistical
Protein Conformation
Selenomethionine - chemistry
Streptomyces coelicolor - metabolism
Structural Genomics Communications
X-Ray Diffraction
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Description
Summary: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% (Rfree = 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.
ISSN:1744-3091
2053-230X
1744-3091
2053-230X
DOI:10.1107/S1744309105019743