Crystallization and preliminary X-ray crystallographic data withEscherichia colitransketolase

Autor:	Jennifer A. Littlechild, G. R. Hobbs, A. Rawas, Herman C. Watson, Nicholas J. Turner, Malcolm D. Lilly
Rok vydání:	1995
Předmět:	chemistry.chemical_classification Dimer General Medicine Transketolase medicine.disease_cause Yeast Enzyme structure Amino acid chemistry.chemical_compound Crystallography Enzyme chemistry Structural Biology medicine Molecular replacement Escherichia coli
Zdroj:	Acta Crystallographica Section D Biological Crystallography. 51:1074-1076
ISSN:	0907-4449
DOI:	10.1107/s0907444995005415
Popis:	The Escherichia coli enzyme transketolase, a dimeric protein of 2 x 70 kDa (662 amino acids) has been prepared from an overexpression system in E. coli. The purified enzyme has been crystallized from PIPES buffer pH 6.4 and ammonium sulfate. The crystals which grow as large plates diffract to greater than 1.9 A, resolution and are of the space group P2(1)2(1)2(1) with unit-cell dimensions of a = 74.6, b = 125.6 and c = 151.0 A, (Z = 8 with one transketolase dimer in the asymmetric unit). The structure has been solved by molecular replacement using the yeast transketolase enzyme structure as a search model. The enzyme is being used for large-scale biotransformations using various aldehydes and hydroxypyruvate as substrates.
Databáze:	OpenAIRE
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