Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104

doi:10.1107/S1744309107038328

Title: Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104

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Abstract

A 40 kDa N-terminal fragment of Saccharomyces cerevisiae Hsp104 was crystallized in two different crystal forms. Native 1 diffracted to 2.6 {angstrom} resolution and belonged to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 66.6, b = 75.8, c = 235.7 {angstrom}. Native 2 diffracted to 2.9 {angstrom} resolution and belonged to space group P6{sub 1}22 or P6{sub 5}22, with unit-cell parameters a = 179.1, b = 179.1, c = 69.7 {angstrom}. This is the first report of the crystallization of a eukaryotic member of the Hsp100 family of molecular chaperones.

Authors:: Lee,S.; Tsai, F.

Publication Date:: Mon Jan 01 00:00:00 EST 2007

Research Org.:: Brookhaven National Laboratory (BNL) National Synchrotron Light Source

Sponsoring Org.:: Doe - Office Of Science

OSTI Identifier:: 930006

Report Number(s):: BNL-80619-2008-JA
TRN: US200822%%957

DOE Contract Number:: DE-AC02-98CH10886

Resource Type:: Journal Article

Resource Relation:: Journal Name: Acta Crystallographica Section F: Structural Biology and Crystallization Communications; Journal Volume: 63

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; CRYSTALLIZATION; CRYSTALS; RESOLUTION; SACCHAROMYCES CEREVISIAE; SPACE GROUPS; YEASTS; X-RAY DIFFRACTION; national synchrotron light source

Citation Formats


                    Lee,S., and Tsai, F.. Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104.  United States: N. p., 2007. 
        Web.  doi:10.1107/S1744309107038328.

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                    Lee,S., & Tsai, F.. Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104.  United States.  doi:10.1107/S1744309107038328.

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                    Lee,S., and Tsai, F.. Mon .  
        "Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104".  United States.  
        doi:10.1107/S1744309107038328.

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@article{osti_930006,

  title        = {Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104},

  author       = {Lee,S. and Tsai, F.},

  abstractNote = {A 40 kDa N-terminal fragment of Saccharomyces cerevisiae Hsp104 was crystallized in two different crystal forms. Native 1 diffracted to 2.6 {angstrom} resolution and belonged to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 66.6, b = 75.8, c = 235.7 {angstrom}. Native 2 diffracted to 2.9 {angstrom} resolution and belonged to space group P6{sub 1}22 or P6{sub 5}22, with unit-cell parameters a = 179.1, b = 179.1, c = 69.7 {angstrom}. This is the first report of the crystallization of a eukaryotic member of the Hsp100 family of molecular chaperones.},

  doi          = {10.1107/S1744309107038328},

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

  number       = ,

  volume       = 63,

  place        = {United States},

  year         = {Mon Jan 01 00:00:00 EST 2007},

  month        = {Mon Jan 01 00:00:00 EST 2007}

}

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DOI: 10.1107/S1744309107038328

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