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Article

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

Molecular biotechnology - 1 Jun 2004

Park Hyun-Woo, Federici Brian A

Abstract excerpt

Insecticidal crystal (Cry) proteins of Bacillus thuringiensis crystallize after synthesis forming large inclusions that stabilize these toxins in the environment after cell lysis until eaten by an insect. Despite the biological importance of crystallization, little is known about the structural elements of Cry molecules that facilitate this process. We identified subdomains that affect Cry3A structure possibly...

Topics

Amino Acid Sequence
Bacillus thuringiensis
Bacillus thuringiensis Toxins
Bacterial Proteins
Bacterial Toxins
Biotechnology
Circular Dichroism
Crystallography, X-Ray
Electrophoresis, Polyacrylamide Gel
Endotoxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Hemolysin Proteins

Microscopy, Electron, Scanning

Microscopy, Phase-Contrast

Molecular Sequence Data

Mutagenesis

Mutagenesis, Site-Directed

Mutation

Plasmids

Source

Identifiers

PMID: 15208451
DOI: 10.1385/MB:27:2:089

Provenance

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Effect of specific mutations in helix alpha7 of domain I on the stability and crystallization of Cry3A in Bacillus thuringiensis.PMID 15208451Read ↗

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