Systematic Variation in DNA Length Yields Highly Ordered Repressor-Operator Cocrystals
- 20 December 1985
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 230 (4732), 1383-1385
- https://doi.org/10.1126/science.3906896
Abstract
Crystals have been grown that contain the operator-binding domain of the lambda repressor and the lambda operator site OL1. Crystallization conditions were tested with a set of DNA fragments, ranging in length from 17 to 23 base pairs. The best crystals were grown with a 20-base pair DNA fragment. These crystals have space-group symmetry P2I, with unit cell dimensions a = 37.1 A, b = 68.8 A, c = 56.8 A, and a beta angle of 91.5 degrees. They diffracted to at least 2.5 A resolution. High resolution data from these crystals should allow the direct determination of how a repressor recognizes its operator site.This publication has 23 references indexed in Scilit:
- The three-dimensional structure of trp repressorNature, 1985
- A phage repressor–operator complex at 7 Å resolutionNature, 1985
- PROTEIN-DNA RECOGNITIONAnnual Review of Biochemistry, 1984
- Kinked DNA in crystalline complex with EcoRI endonucleaseNature, 1984
- 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 a B-DNA dodecamerJournal of Molecular Biology, 1981
- Optimised parameters for A-DNA and B-DNABiochemical and Biophysical Research Communications, 1972
- Solvent content of protein crystalsJournal of Molecular Biology, 1968