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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 12
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pubmed:dateCreated |
2007-12-17
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pubmed:abstractText |
Past work has shown that it is feasible to mutate surface residues of soluble proteins and to a lesser extent membrane proteins in order to improve their crystallization behavior. Described here is a successful application of this approach to the integral membrane protein Thermus thermophilus cytochrome ba(3) oxidase. Two mutant forms of this enzyme (I-K258R and I-K258R/II-E4Q) were created in which symmetrical crystal contacts within crystals of wild-type enzyme were modified. These mutant proteins had greatly shortened crystallization times, decreasing from approximately 30 d for the wild type to 1-3 d for the mutants, and crystallization was highly reproducible. Native-like proteins crystallize in space group P4(3)2(1)2, whereas the mutant proteins crystallize in space group P4(1)2(1)2 with a different packing arrangement. Crystals of the P4(3)2(1)2 form occasionally diffracted to 2.4-2.3 A resolution following controlled dehydration, while those of the P4(1)2(1)2 form routinely diffracted to between 3.0 and 2.6 A for crystals that had been cryoprotected but not dehydrated.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-10022352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-10489468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-10531519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-10545325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-10764596,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-10775261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-11320308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-11567148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-12163074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-12454455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-14747703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-15062076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-15299464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-15325653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-15735345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-15766872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-15858260,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-16369101,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-16828701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-17050682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-17050688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-17452789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-1992356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-7552705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-8638158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-8749850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-9261866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-9345629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-9380672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18084085-9646871
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1029-34
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pubmed:dateRevised |
2010-9-21
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pubmed:meshHeading |
pubmed-meshheading:18084085-Crystallization,
pubmed-meshheading:18084085-Crystallography, X-Ray,
pubmed-meshheading:18084085-Cytochrome b Group,
pubmed-meshheading:18084085-Membrane Proteins,
pubmed-meshheading:18084085-Models, Molecular,
pubmed-meshheading:18084085-Mutation,
pubmed-meshheading:18084085-Oxidoreductases,
pubmed-meshheading:18084085-Protein Engineering,
pubmed-meshheading:18084085-Protein Structure, Quaternary,
pubmed-meshheading:18084085-Protein Structure, Tertiary,
pubmed-meshheading:18084085-Protein Subunits,
pubmed-meshheading:18084085-Recombinant Proteins,
pubmed-meshheading:18084085-Structural Homology, Protein,
pubmed-meshheading:18084085-Thermus thermophilus
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pubmed:year |
2007
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pubmed:articleTitle |
An unexpected outcome of surface engineering an integral membrane protein: improved crystallization of cytochrome ba(3) from Thermus thermophilus.
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pubmed:affiliation |
The Scripps Research Institute, Department of Molecular Biology, MB-8, 10550 North Torrey Pines Road, La Jolla CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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