Article
Crystallization of genetically engineered active maltose-binding proteins, including an immunogenic viral epitope insertion.
Journal of molecular biology - 20 Jun 1990
Rodseth L E, Martineau P, Duplay P, Hofnung M, Quiocho F A
Abstract excerpt
Three mutants of the maltose- or maltodextrin-binding protein encoded by the malE gene of Escherichia coli, with extensive genetic changes, have been purified and crystallized in different crystal forms. Two of these mutant proteins, MalE178 and MalE341, carry net deletions of seven and 13 residu...
Topics
- ATP-Binding Cassette Transporters
- Amino Acid Sequence
- Biological Transport
- Capsid
- Capsid Proteins
- Carrier Proteins
- Crystallization
- Epitopes
- Escherichia coli
- Escherichia coli Proteins
- Genetic Engineering
- Maltose
- Maltose-Binding Proteins
- Molecular Sequence Data
- Monosaccharide Transport Proteins
- Mutation
- Periplasmic Binding Proteins
- Poliovirus