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 Å and belong to space group P4 2 , with unit-cell parameters a = b = 101.92, c = 100.28 Å and two molecules per asymmetric unit. Phasing was successfully performed by molecular replacement.
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Essential hypertension is an important cause of cardiovascular morbidity and mortality worldwide with
significant clinical and economical implications. The field of antihypertensive treatment already numbers numerous agents
and class of drugs. However, despite these, patients are still developing uncontrolled hypertension hence the continuous
need for novel agents, with good tolerability. Advances in this field are focussing both on pharmacotherapy, with
developments in traditional and non-traditional targets, as well as interventional techniques such as renal denervation and
baroreflex activation therapy. It is likely that future strategies may involve a tailored approach to the individual patient, with
genetic modulation playing a key role.
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