The expression, purification and crystallization of a ubiquitin-conjugating enzyme E2 from Agrocybe aegerita underscore the impact of His-tag location on recombinant protein properties

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 69, Issue 2, 2013, Pages 153-157

  Li, De Feng ^a   Feng, Lei ^a   Hou, Yan Jie ^a   Liu, Wei ^b  

^a INSTITUTE OF BIOPHYSICS   (China)

^b THIRD MILITARY MEDICAL UNIVERSITY   (China)

Author keywords

Agrocybe aegerita; UbcA1; ubiquitin; ubiquitin conjugating enzyme E2

Indexed keywords

HIS HIS HIS HIS HIS HIS; HIS-HIS-HIS-HIS-HIS-HIS; HISTIDINE; OLIGOPEPTIDE; RECOMBINANT PROTEIN; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME;

AGROCYBE; AGROCYBE AEGERITA; ARTICLE; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; POLYACRYLAMIDE GEL ELECTROPHORESIS; UBCA1; UBIQUITIN-CONJUGATING ENZYME E2; X RAY CRYSTALLOGRAPHY;

AGROCYBE AEGERITA; UBCA1; UBIQUITIN; UBIQUITIN-CONJUGATING ENZYME E2;

AGROCYBE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HISTIDINE; OLIGOPEPTIDES; RECOMBINANT PROTEINS; UBIQUITIN-CONJUGATING ENZYMES;

EID: 84873583060     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309112051755     Document Type: Article

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