Supplementary Materials

Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state

Joost Snijder, Jan M. Schuller, Anika Wiegard, Philip Lössl, Nicolas Schmelling, Ilka M. Axmann, JuÌ^rgen M. Plitzko, Friedrich Förster, Albert J. R. Heck

Materials/Methods, Supplementary Text, Tables, Figures, and/or References

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  • Materials and Methods
  • Figs. S1 to S15
  • Captions for Tables S1 to S4
  • Captions for Data S1 to S3
  • References
Table S1
Masses of identified Kai protein and protein complex species. The molecular weights of the monomeric Kai proteins are shown in parentheses. Note that the residual masses expressed as mass deviation (%) originate from a small amount of residual buffer and solvent that remains attached to the ions, as routinely observed in native MS experiments.
Table S2
Unique crosslinks identified within the KaiCBA complex. Listed are charge state, mass and number of peptide spectrum matches (PSMs) for each crosslinked peptide pair. The crosslinked peptides (α and β) are individually characterized by their amino acid sequence (o = Met oxidation), the positions of the linked Lys residues, their molecular weight, the number of matched fragment ions (nonintegral numbers indicate a fragment ion matching to both peptides) and the N scores, as calculated by XlinkX.
Table S3
Fractional changes in Deuterium uptake of KaiA, KaiB and KaiC as free components compared to KaiCB and KaiCBA assemblies. The list includes all confidently identified peptides ordered by primary sequence on the protein level.
Table S4
Primers used for mutagenesis. Small letters indicate the inserted mutations resulting in exchange of single amino acids.
Deuterium uptake plots for all KaiA (Data S1), KaiB (Data S2) and KaiC (Data S3) peptides included in the analysis. Error bars represent standard deviations
Data S1
Data S2
Data S3