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Crystallization of recombinant bifunctional nuclease TBN1 from tomato
T. Koval', P. Lipovová, T. Podzimek, J. Matoušek, J. Dušková, T. Skálová, A. Stěpánková, J. Hašek, J. Dohnálek
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 2005 do 2013
PubMed Central
od 2005 do 2013
Europe PubMed Central
od 2005 do 2013
Wiley Online Library (archiv)
od 2005-01-01 do 2012-12-31
- MeSH
- deoxyribonukleasy chemie genetika MeSH
- ionty chemie MeSH
- konformace proteinů MeSH
- krystalizace MeSH
- krystalografie rentgenová MeSH
- molekulární sekvence - údaje MeSH
- rekombinantní proteiny chemie genetika MeSH
- rostlinné proteiny chemie genetika MeSH
- Solanum lycopersicum chemie genetika MeSH
- zinek chemie MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
The endonuclease TBN1 from Solanum lycopersicum (tomato) was expressed in Nicotiana benthamiana leaves and purified with suitable quality and in suitable quantities for crystallization experiments. Two crystal forms (orthorhombic and rhombohedral) were obtained and X-ray diffraction experiments were performed. The presence of natively bound Zn2+ ions was confirmed by X-ray fluorescence and by an absorption-edge scan. X-ray diffraction data were collected from the orthorhombic (resolution of 5.2 Å) and rhombohedral (best resolution of 3.2 Å) crystal forms. SAD, MAD and MR methods were applied for solution of the phase problem, with partial success. TBN1 contains three Zn2+ ions in a similar spatial arrangement to that observed in nuclease P1 from Penicillium citrinum.
Institute of Biotechnology CAS v v i Vídeňská 1083 142 20 Praha 4 Czech Republic
Institute of Macromolecular Chemistry AS CR vvi Heyrovsky sq 2 162 06 Prague 6 Czech Republic
Institute of Physics AS CR v v i Na Slovance 2 182 21 Praha 8 Czech Republic
University of Chemistry and Technology Technická 5 166 28 Praha 6 Czech Republic
Citace poskytuje Crossref.org
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