Article
Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysis.
Journal of molecular biology - 17 Oct 1997
Perona J J, Martin A M
Abstract excerpt
The structures of wild-type and mutant forms of the unliganded EcoRV endonuclease dimer have been determined at 2.4 A resolution in a new crystal lattice. Comparison of these structures with that of the free enzyme determined with different packing constraints shows that the conformations of the domain interfaces are not conserved between crystal forms. The unliganded enzyme and the enzyme-DNA complex delineate...
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