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ABSTRACT:
SUBMITTER: Meramveliotaki C
PROVIDER: S-EPMC2339719 | biostudies-literature | 2007 Oct
REPOSITORIES: biostudies-literature
Acta crystallographica. Section F, Structural biology and crystallization communications 20070919 Pt 10
The restriction endonuclease PvuII from Proteus vulgaris has been converted from its wild-type homodimeric form into the enzymatically active single-chain variant scPvuII by tandemly joining the two subunits through the peptide linker Gly-Ser-Gly-Gly. scPvuII, which is suitable for the development of programmed restriction endonucleases for highly specific DNA cleavage, was purified and crystallized. The crystals diffract to a resolution of 2.35 A and belong to space group P4(2), with unit-cell ...[more]