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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1993-3-16
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pubmed:abstractText |
For two-dimensional (2-D) crystallization we have purified the molecular chaperone GroEL from Escherichia coli to homogeneity. The final and important step for crystallization in the purification procedure was an ATP-agarose column, on which the spacer between ATP and agarose was attached to C8 of adenine. Using the mica spreading "negative staining-carbon film" procedure and polyethylene glycol as a precipitant, we obtained four different 2-D periodic arrays. Two of them turned out to be true crystals. One crystal has P2 symmetry and lattice constants of a = 24.3 nm and b = 16.9 nm, the other has essentially P4 symmetry and shows smoothly varying local changes in the lattice parameters (a = b = 23 (+/- 1.3) nm). Very striking in the P4 crystal is the departure within each individual GroEL particle from the GroEL-typical seven-fold symmetry, which seems to be required for GroEL to accommodate to a crystal symmetry.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
229
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
579-84
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading | |
pubmed:year |
1993
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pubmed:articleTitle |
Two-dimensional crystals of the molecular chaperone GroEL reveal structural plasticity.
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pubmed:affiliation |
Protein Engineering Group, Max-Planck-Institut für Biochemie Am Klopferspitz, Martinsried, Germany.
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pubmed:publicationType |
Journal Article
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