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Crystallization And X-Ray Crystallographic Studies Of An Inhibitor From Rye (Secale Cereale) Active Against Acanthoscelides Obtectus And Zabrotes Subfasciatus Alpha-Amylases

Iulek, Jorge ; Slivinskic, Christiane Trevisan ; Silva, Márcio

Protein and peptide letters, 2004-02, Vol.11 (1), p.79-83 [Periódico revisado por pares]

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Crystallization And X-Ray Crystallographic Studies Of An Inhibitor From Rye (Secale Cereale) Active Against Acanthoscelides Obtectus And Zabrotes Subfasciatus Alpha-Amylases
Autor: Iulek, Jorge ; Slivinskic, Christiane Trevisan ; Silva, Márcio
Assuntos: alpha-Amylases - antagonists & inhibitors ; alpha-Amylases - metabolism ; Animals ; Coleoptera - enzymology ; Crystallization ; Crystallography, X-Ray ; Enzyme Inhibitors - chemistry ; Enzyme Inhibitors - isolation & purification ; Secale - chemistry
É parte de: Protein and peptide letters, 2004-02, Vol.11 (1), p.79-83
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: Crystals of a new inhibitor present in rye seeds active against alpha-amylases from crop pests Acanthoscelides obtectus and Zabrotes subfasciatus have been obtained. A native dataset was collected at 2.21 Å resolution with 99.3 % completeness at CPr beamline at LNLS. The crystals belong to the trigonal system, space group P3121 with a = b = 78.21 Å, and c = 59.61 Å. The crystal calculated solvent content is compatible with one dimer per asymmetric unit.
Editor: Netherlands: Bentham Science Publishers Ltd
Idioma: Inglês

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