Using rational screening and electron microscopy to optimize the crystallization of succinate:ubiquinone oxidoreductase from Escherichia coli.
Acta Crystallogr D Biol Crystallogr
; 59(Pt 3): 600-2, 2003 Mar.
Article
in En
| MEDLINE
| ID: mdl-12595738
ABSTRACT
The membrane-bound respiratory complex II, succinateubiquinone oxidoreductase (SQR) from Escherichia coli, has been anaerobically expressed, then purified and crystallized. The initial crystals obtained were small and diffracted poorly. In order to facilitate structure determination, rational screening and sample-quality analysis using electron microscopy was implemented. The crystals of SQR from E. coli belong to the trigonal space group R32, with unit-cell parameters a = b = 138.7, c = 521.9 A, and diffract to 2.6 A resolution. The optimization strategy used for obtaining well diffracting SQR crystals is applicable to a wide range of membrane proteins.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Oxidoreductases
/
Succinate Dehydrogenase
/
Escherichia coli
/
Multienzyme Complexes
Type of study:
Diagnostic_studies
/
Screening_studies
Language:
En
Journal:
Acta Crystallogr D Biol Crystallogr
Year:
2003
Document type:
Article
Affiliation country:
United kingdom