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Structure paper

TitleProline/alanine-rich sequence (PAS) polypeptides as an alternative to PEG precipitants for protein crystallization.
Journal, issue, pagesActa Crystallogr. ,Sect. F, Vol. 76, Page 320-325, Year 2020
Publish dateApr 5, 2020 (structure data deposition date)
AuthorsSchiefner, A. / Walser, R. / Gebauer, M. / Skerra, A.
External linksActa Crystallogr. ,Sect. F / PubMed:32627748
MethodsX-ray diffraction
Resolution1.2 - 2.1 Å
Structure data

PDB-6yjw:
Structure of Fragaria ananassa O-methyltransferase crystallized with PAS polypeptide
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-6yjx:
Structure of Hen egg-white lysozyme crystallized with PAS polypeptide
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-ACT:
ACETATE ION

Source
  • fragaria ananassa (strawberry)
  • gallus gallus (chicken)
KeywordsTRANSFERASE / PAS polypeptide / P/A200 / precipitant / proline-alanine rich sequence / protein crystallization / HYDROLASE

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