Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals

Protein Science

Volumn 23, Issue 11, 2014, Pages 1491-1497

  Evdokimov, Artem G ^a   Moshiri, Farhad ^a   Sturman, Eric J ^a   Rydel, Timothy J ^a   Zheng, Meiying ^a   Seale, Jeffrey W ^a   Franklin, Sonya ^a  

^a MONSANTO COMPANY   (United States)

Author keywords

Bacillus thuringiensis; Cry1A; insecticidal toxin; insecticidal toxin mode of action; natural crystal packing; structure of full length toxin

Indexed keywords

CARBOHYDRATE DERIVATIVE; CRY1AC TOXIN; CYSTEINE DERIVATIVE; DIMER; MONOMER; BACTERIAL PROTEIN; ENDOTOXIN; HEMOLYSIN; INSECTICIDAL CRYSTAL PROTEIN, BACILLUS THURINGIENSIS; INSECTICIDE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CROSS LINKING; CRYSTAL STRUCTURE; CRYSTALLIZATION; ELECTRON MICROSCOPY; ESCHERICHIA COLI; GEL FILTRATION; IN VITRO STUDY; IN VIVO STUDY; INSECTICIDAL ACTIVITY; LIGHT SCATTERING; MICROSPOROGENESIS; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLUBILIZATION; SPOROGENESIS; X RAY DIFFRACTION; CHEMICAL STRUCTURE; CHEMISTRY; PROTEIN CONFORMATION;

BACILLUS THURINGIENSIS;

BACTERIAL PROTEINS; ENDOTOXINS; HEMOLYSIN PROTEINS; INSECTICIDES; MODELS, MOLECULAR; PROTEIN CONFORMATION; RECOMBINANT PROTEINS;

EID: 84919833320     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2536     Document Type: Article

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