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Efficient expression, purification and crystallisation of two hyperthermostable enzymes of histidine biosynthesis.

Thoma, Ralf, Obmolova, G., Lang, D. A., Schwander, M., Jenö, P., Sterner, Reinhard and Wilmanns, Matthias (1999) Efficient expression, purification and crystallisation of two hyperthermostable enzymes of histidine biosynthesis. FEBS letters 454 (1-2), pp. 1-6.

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Abstract

Enzymes from hyperthermophiles can be efficiently purified after expression in mesophilic hosts and are well-suited for crystallisation attempts. Two enzymes of histidine biosynthesis from Thermotoga maritima, N'-((5'-phosphoribosyl)-formimino)-5-aminoimidazol-4-carb oxamid ribonucleotide isomerase and the cyclase moiety of imidazoleglycerol phosphate synthase, were overexpressed in Escherichia ...

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Item type:Article
Date:1999
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
10413084PubMed ID
Classification:
NotationType
Aldose-Ketose Isomerases/isolation & purificationMESH
Aminohydrolases/isolation & purificationMESH
Bacterial Proteins/isolation & purificationMESH
Chromatography, High Pressure LiquidMESH
CrystallizationMESH
Crystallography, X-RayMESH
Histidine/biosynthesisMESH
Mass SpectrometryMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:13705
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