Abstract
A 40 kDa N-terminal fragment of Saccharomyces cerevisiae Hsp104 was crystallized in two different crystal forms. Native 1 diffracted to 2.6 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 66.6, b = 75.8, c = 235.7 A. Native 2 diffracted to 2.9 A resolution and belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = 179.1, b = 179.1, c = 69.7 A. This is the first report of the crystallization of a eukaryotic member of the Hsp100 family of molecular chaperones.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / isolation & purification
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray
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Escherichia coli
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Heat-Shock Proteins / chemistry*
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Heat-Shock Proteins / isolation & purification
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Peptide Fragments / chemistry
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / isolation & purification
Substances
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Heat-Shock Proteins
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Peptide Fragments
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Recombinant Proteins
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Saccharomyces cerevisiae Proteins
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HsP104 protein, S cerevisiae
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Adenosine Triphosphatases