| dc.contributor.author |
Meramveliotaki, C |
en |
| dc.contributor.author |
Kotsifaki, D |
en |
| dc.contributor.author |
Androulaki, M |
en |
| dc.contributor.author |
Hountas, A |
en |
| dc.contributor.author |
Eliopoulos, E |
en |
| dc.contributor.author |
Kokkinidis, M |
en |
| dc.date.accessioned |
2014-06-06T06:47:55Z |
|
| dc.date.available |
2014-06-06T06:47:55Z |
|
| dc.date.issued |
2007 |
en |
| dc.identifier.issn |
17443091 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1107/S1744309107040377 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/3861 |
|
| dc.subject |
Programmed restriction endonucleases |
en |
| dc.subject |
PvuII |
en |
| dc.subject |
ScPvuII |
en |
| dc.subject.other |
endodeoxyribonuclease PvuII |
en |
| dc.subject.other |
recombinant protein |
en |
| dc.subject.other |
type II site specific deoxyribonuclease |
en |
| dc.subject.other |
unclassified drug |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
chemistry |
en |
| dc.subject.other |
crystallization |
en |
| dc.subject.other |
enzymology |
en |
| dc.subject.other |
Escherichia coli |
en |
| dc.subject.other |
genetics |
en |
| dc.subject.other |
isolation and purification |
en |
| dc.subject.other |
methodology |
en |
| dc.subject.other |
protein engineering |
en |
| dc.subject.other |
Proteus vulgaris |
en |
| dc.subject.other |
X ray diffraction |
en |
| dc.subject.other |
Crystallization |
en |
| dc.subject.other |
Deoxyribonucleases, Type II Site-Specific |
en |
| dc.subject.other |
Escherichia coli |
en |
| dc.subject.other |
Protein Engineering |
en |
| dc.subject.other |
Proteus vulgaris |
en |
| dc.subject.other |
Recombinant Proteins |
en |
| dc.subject.other |
X-Ray Diffraction |
en |
| dc.subject.other |
Proteus vulgaris |
en |
| dc.title |
Purification, crystallization, X-ray diffraction analysis and phasing of an engineered single-chain PvuII restriction endonuclease |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1107/S1744309107040377 |
en |
| heal.publicationDate |
2007 |
en |
| heal.abstract |
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 P42, 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. © International Union of Crystallography 2007. |
en |
| heal.journalName |
Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
en |
| dc.identifier.issue |
10 |
en |
| dc.identifier.volume |
63 |
en |
| dc.identifier.doi |
10.1107/S1744309107040377 |
en |
| dc.identifier.spage |
836 |
en |
| dc.identifier.epage |
838 |
en |