Crystallographic data for complexes of the Cro repressor with DNA
- 25 August 1983
- journal article
- other
- Published by Elsevier in Journal of Molecular Biology
- Vol. 168 (4) , 903-906
- https://doi.org/10.1016/s0022-2836(83)80082-5
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Solvent content of protein crystalsPublished by Elsevier ,2006
- Many gene-regulatory proteins appear to have a similar α-helical fold that binds DNA and evolved from a common precursorJournal of Molecular Evolution, 1983
- Proposed α-helical super-secondary structure associated with protein-DNA recognitionJournal of Molecular Biology, 1982
- The molecular basis of DNA–protein recognition inferred from the structure of cro repressorNature, 1982
- Homology among DNA-binding proteins suggests use of a conserved super-secondary structureNature, 1982
- The operator-binding domain of λ repressor: structure and DNA recognitionNature, 1982
- Structure of the cro repressor from bacteriophage λ and its interaction with DNANature, 1981
- Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNANature, 1981
- Solid-phase synthesis of polynucleotides. IV. Usage of polystyrene resins for the synthesis of polydeoxyribonucleotides by the phosphotriester methodNucleic Acids Research, 1980
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976