Characterization and crystallization of an active N-terminally truncated form of the Escherichia coli glycogen branching enzyme

European Journal of Biochemistry

Volumn 267, Issue 8, 2000, Pages 2150-2155

  Hilden, Ida ^a,b   Leggio, Leila L ^c   Larsen, Sine ^c   Poulsen, Peter ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b DANISCO A S   (Denmark)

^c NONE

Author keywords

Amylolytic enzymes; Crystallization; Enzyme solubility

Indexed keywords

1,4 ALPHA GLUCAN BRANCHING ENZYME; AMYLASE; AMYLOSE; PHOSPHORYLASE;

ARTICLE; CRYSTALLIZATION; ENZYME PURIFICATION; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE EXPRESSION; MASS SPECTROMETRY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SOLUBILITY;

1,4-ALPHA-GLUCAN BRANCHING ENZYME; AMYLOSE; BACTERIAL PROTEINS; CRYSTALLIZATION; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; ISOENZYMES; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS; SUBSTRATE SPECIFICITY; X-RAY DIFFRACTION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PROKARYOTA;

EID: 0034052144     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01221.x     Document Type: Article

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