README for Figure4A_data.csv

*** This file contains the raw data obtained on DNA-HMfA and DNA-HMfAK31A E34A complexes using magnetic tweezers as represented in Figure 4A of

Article: Mechanical and structural properties of archaeal hypernucleosomes
Authors: Henneman, Brouwer, Erkelens, Kuijntjes, van Emmerik, van der Valk, Timmer, Kirolos, van Ingen, van Noort, Dame
Journal: Nucleic Acids Research
DOI: 10.1093/nar/gkaa1196
Corresponding authors: rtdame@chem.leidenuniv.nl and noort@physics.leidenuniv.nl

Legend Figure 4) Mutations in the stacking interface of HMfA and HMfB destabilize the hypernucleosome. A) DNA-protein complexes of HMfAK31A E34A show similar compaction as wt HMfA below 0.5 pN, but unfold at lower force. The pink curve shows the wt data. Note that HMfAK31A E34A does not feature a second unfolding plateau. Grey circles show the refolding curve, which overlaps with the unfolding data.  Solid lines show fits to equation 10. The mutant features a reduced stiffness, stacking energy, wrapping energy and deflection angle, suggesting that the mutations not only affect stacking but also wrapping of DNA  B) DNA-protein complexes of HMfBD14A K30A E34A show similar stretching behavior as the HMfA mutant, but unfold at slightly lower force. A representative curve of wt HMfB is plotted in light blue. The fits show the same trend as for HMfA, but the mutations have a stronger effect, yielding similar mechanical properties for both mutants. Fit parameters are listed in table 2.

*** The data were obtained using Magnetic Tweezers as described in the associated article.

*** Columns show F (Force in pN) and z (Distance in micrometer) of DNA-HMfA and DNA-HMfAK31A E34A complexes
