Crystal structure analysis of a mutant Escherichia coli thioredoxin in which lysine 36 is replaced by glutamic acid

The structure of a mutant Escherichia coli thioredoxin with a glutamic acid substituted for a conserved lysine at position 36 adjacent to the active site has been solved using molecular replacement and refined at 2.0-A resolution to a crystallographic residual of 19.9%. The mutant was crystallized i...

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Veröffentlicht in:	Biochemistry (Easton) 1993-05, Vol.32 (19), p.5093-5098
Hauptverfasser:	Nikkola, Matti, Gleason, Florence K, Fuchs, James A, Eklund, Hans
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Binding Sites Biological and medical sciences Copper - metabolism Crystallization Disulfides - chemistry Drug Stability Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - chemistry Fundamental and applied biological sciences. Psychology Glutamates Glutamic Acid Hydrogen Bonding Lysine Molecular Structure Mutagenesis Oxidoreductases Protein Conformation Solvents Spectrometry, Fluorescence Thioredoxins - chemistry Thioredoxins - genetics Thioredoxins - metabolism X-Ray Diffraction
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