9PIS: Ab initio structure of crambin by MicroED

Ab initio structure of crambin by MicroED at 0.85A. Determined by electron crystallography at 0.85 Å resolution. Released 25 Feb 2026.

Method
Electron crystallography
Resolution
0.85 Å
Organism
Crambe hispanica subsp. abyssinica
Chains
1
Atoms
435
Mol. weight
4.73 kDa
Released
25 Feb 2026

Explore 9PIS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9PIS contains 2 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 2 β-strands

ElementResiduesLengthSheet
β-strand2-321
α-helix7-1711
α-helix23-308
β-strand33-3421

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CrambinAprotein46Crambe hispanica subsp. abyssinicaP01542 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9PIS_1 Crambin (chains A)
TTCCPSIVARSNFNVCRLPGTSEAICATYTGCIIIPGATCPGDYAN

Primary citation

Direct from the seed: an atomic resolution protein structure by ab initio MicroED. Vasireddy, P.C.R., Low-Beer, T., Spoth, K.A. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-69601-y · PubMed

Other PDB entries of the same protein (UniProt P01542 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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