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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-3-16
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
229
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
579-84
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Two-dimensional crystals of the molecular chaperone GroEL reveal structural plasticity.
pubmed:affiliation
Protein Engineering Group, Max-Planck-Institut für Biochemie Am Klopferspitz, Martinsried, Germany.
pubmed:publicationType
Journal Article