Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation.

Journal of molecular biology - 1 Dec 1995

Grochulski P, Masson L, Borisova S, Pusztai-Carey M, Schwartz J L, Brousseau R, Cygler M

Abstract excerpt

The activated 65 kDa lepidopteran-specific CryIA(a) toxin from the commercially most important strain Bacillus thuringiensis var. kurstaki HD-1 has been investigated by X-ray diffraction and for its ability to form channels in planar lipid bilayers. Its three-dimensional structure has been determined by a multiple isomorphous replacement method and refined at 2.25 A resolution to an R-factor of 0.168 for data...

Topics

Bacillus thuringiensis
Bacillus thuringiensis Toxins
Bacterial Proteins
Bacterial Toxins
Conserved Sequence
Crystallography, X-Ray
DNA Mutational Analysis
Endotoxins
Hemolysin Proteins
Insect Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Ion Channels

Lipid Bilayers

Models, Molecular

Mutation

Pest Control, Biological

Protein Binding

Protein Conformation

Protein Folding

Source

Identifiers

PMID: 7490762
DOI: 10.1006/jmbi.1995.0630

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7490762-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation.PMID 7490762Read ↗

Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications.Semantic proximity Read ↗

Structural and functional studies of alpha-helix 5 region from Bacillus thuringiensis Cry1Ab delta-endotoxin.Semantic proximity Read ↗

Analysis of mutations in the pore-forming region essential for insecticidal activity of a Bacillus thuringiensis delta-endotoxin.Semantic proximity Read ↗

Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection.Semantic proximity Read ↗

Characterization of the mechanism of action of the genetically modified Cry1AbMod toxin that is active against Cry1Ab-resistant insects.Semantic proximity Read ↗

Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane.Semantic proximity Read ↗

Effect of specific mutations in helix alpha7 of domain I on the stability and crystallization of Cry3A in Bacillus thuringiensis.Semantic proximity Read ↗

Specific mutations within the alpha4-alpha5 loop of the Bacillus thuringiensis Cry4B toxin reveal a crucial role for Asn-166 and Tyr-170.Semantic proximity Read ↗

All domains of Cry1A toxins insert into insect brush border membranes.Semantic proximity Read ↗

Bacillus thuringiensis Cry1Ab mutants affecting oligomer formation are non-toxic to Manduca sexta larvae.Semantic proximity Read ↗

Enhancement of Bacillus thuringiensis Cry1Ab and Cry1Fa Toxicity to Spodoptera frugiperda by Domain III Mutations Indicates There Are Two Limiting Steps in Toxicity as Defined by Receptor Binding and Protein Stability.Semantic proximity Read ↗

Rearrangement of N-Terminal α-Helices of Bacillus thuringiensis Cry1Ab Toxin Essential for Oligomer Assembly and Toxicity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.