Abstract
A new high resolution crystal structure of the phage λ repressor reveals the basis for repressor dimer formation and, together with biochemical data, provides insights into the mechanism of repressor tetramer formation, a process essential to the cooperative binding and gene regulatory activities of this protein.
| Original language | English |
|---|---|
| Pages (from-to) | R704-R707 |
| Journal | Current Biology |
| Volume | 10 |
| Issue number | 19 |
| DOIs | |
| State | Published - Oct 5 2000 |
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