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Structure paper

TitleBackbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase alpha-subunit from solution-state NMR.
Journal, issue, pagesJ. Biomol. Nmr, Vol. 74, Page 341-354, Year 2020
Publish dateMay 1, 2019 (structure data deposition date)
AuthorsSakhrani, V.V. / Hilario, E. / Caulkins, B.G. / Hatcher-Skeers, M.E. / Fan, L. / Dunn, M.F. / Mueller, L.J.
External linksJ. Biomol. Nmr / PubMed:32415580
MethodsX-ray diffraction
Resolution1.6 - 1.75 Å
Structure data

PDB-6oso:
The crystal structure of the isolate tryptophan synthase alpha-chain from Salmonella enterica serovar typhimurium at 1.75 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-6ouy:
The crystal structure of the isolate tryptophan synthase alpha-chain from Salmonella enterica serovar typhimurium at 1.60 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-HOH:
WATER

Source
  • salmonella enterica subsp. enterica serovar typhimurium str. lt2 (bacteria)
KeywordsLYASE / tryptophan synthase / alpha-chain / wild-type / recombinant protein

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