Crystallization of recombinant bifunctional nuclease TBN1 from tomato
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
21206042
PubMed Central
PMC3079990
DOI
10.1107/s1744309110048177
PII: S1744309110048177
Knihovny.cz E-zdroje
- 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
- Názvy látek
- deoxyribonukleasy MeSH
- ionty MeSH
- rekombinantní proteiny MeSH
- rostlinné proteiny MeSH
- zinek 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.
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