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

Simon T.M. Allard; Craig A. Bingman; Kenneth A. Johnson; Eduard Bitto; Won Bae Jeon; Gary E. Wesenberg; George N. Phillips

doi:10.1107/S1744309105019743

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

Simon T.M. Allard, Craig A. Bingman, Kenneth A. Johnson, Eduard Bitto, Won Bae Jeon, Gary E. Wesenberg, George N. Phillips

Division of Biotechnology

University of Wisconsin-Madison

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	647-650
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	61
Issue number	7
DOIs	https://doi.org/10.1107/S1744309105019743
State	Published - Jul 2005

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title = "Structure at 1.6 {\AA} resolution of the protein from gene locus At3g22680 from Arabidopsis thaliana",

abstract = "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 {\AA} 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.",

author = "Allard, \{Simon T.M.\} and Bingman, \{Craig A.\} and Johnson, \{Kenneth A.\} and Eduard Bitto and Jeon, \{Won Bae\} and Wesenberg, \{Gary E.\} and Phillips, \{George N.\}",

year = "2005",

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doi = "10.1107/S1744309105019743",

language = "English",

volume = "61",

pages = "647--650",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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T1 - Structure at 1.6 Å resolution of the protein from gene locus At3g22680 from Arabidopsis thaliana

AU - Allard, Simon T.M.

AU - Bingman, Craig A.

AU - Johnson, Kenneth A.

AU - Bitto, Eduard

AU - Jeon, Won Bae

AU - Wesenberg, Gary E.

AU - Phillips, George N.

PY - 2005/7

Y1 - 2005/7

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AB - 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.

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SN - 1744-3091

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EP - 650

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 7

ER -

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

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