Archaeal Connectase is a specific and efficient protein ligase related to proteasome β subunits

Published: 10 February 2021| Version 1 | DOI: 10.17632/m3yw9sf8nn.1
Adrian Fuchs


Primary data used in the study on Connectase, a novel protein ligase enzyme. The paper can be found under and is soon to be published by PNAS (will be linked here); the main text and the method section give detailed information on how the data was generated and how it can be interpreted. Supplied here are full images of all polyacrylamide gels, their quantitative analysis and data recorded in mass spectrometry, light scattering and microscale thermophoresis analyses. All files are named to indicate the experiment and/or figure, in which they were used. The polyacrylamide gels are supplied as TIF files and all other data as XLSX tables. The quantification tables include calculated ligation rates as they are plotted in the paper. The tables for the mass spectrometric analyses of the dimethyl labeling and pulldown experiments show all detected peptides, their intensities and further information as indicated by the headers. The tables for the light scattering, liquid chromatography mass spectrometry (LCMS) and microscale thermophoresis experiments contain x/y data used for plots in the paper. In the LCMS tables, x denotes the deconvoluted molecular mass [Da] and y the signal intensity [AU]. In the light scattering tables, x denotes the elution volume [ml] from the column and y the signal intensity [AU] or detected molar mass [DA] as indicated. In the microscale thermophoresis tables, x denotes the substrate concentration [nM] and y the detected signal in three independent experiments or a data fit as approximated by the instrument software.