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Literature summary extracted from

  • Vujicic-Zagar, A.; Dijkstra, B.W.
    Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 A resolution (2006), Acta Crystallogr. Sect. F, 62, 716-721.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.1 hanging-drop vapour diffusion technique at 23°C. Monoclinic crystal (space group P2(1)) form of alpha-amylase in complex with maltose at 1.8 A resolution. A 1.6 A resolution orthorhombic crystal form (space group P2(1)2(1)2) of the native enzyme is presented. Four maltose molecules are observed in the maltose-alpha-amylase complex Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Aspergillus niger
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1
-
Aspergillus niger