Crystallization and preliminary X-ray studies on the co-repressor binding domain of the Escherichia coli purine repressor
- 20 June 1992
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 225 (4) , 1131-1133
- https://doi.org/10.1016/0022-2836(92)90111-v
Abstract
No abstract availableKeywords
This publication has 8 references indexed in Scilit:
- The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis.Published by Elsevier ,2021
- Solvent content of protein crystalsPublished by Elsevier ,2006
- Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding proteinResearch in Microbiology, 1991
- Atomic features of protein-carbohydrate interactionsCurrent Opinion in Structural Biology, 1991
- Purification of the Escherichia coli purine regulon repressor and identification of corepressorsJournal of Bacteriology, 1990
- Autoregulation of Escherichia coli purR requires two control sites downstream of the promoterJournal of Bacteriology, 1990
- The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic libraryCell, 1987
- CARBOHYDRATE-BINDING PROTEINS: TERTIARY STRUCTURES AND PROTEIN-SUGAR INTERACTIONSAnnual Review of Biochemistry, 1986