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App note: Characterizing protein-DNA interactions with mass photometry
In this application note, you will learn how mass photometry, along with MassGlass CC slides, can be used to successfully measure the mass of nucleic acid and protein molecules, and to quantify their abundance and the abundance of complexes they form. You will see a comparison of mass photometry measurements of proteins made using functionalized (MassGlass CC) and non-functionalized slides. Finally, you will see data proving that mass photometry can detect DNA and proteins in complex as well as separately, providing the necessary data to quantify their dissociation constant – with results consistent with SPR.

Additional resources
WEBINAR: Elucidating the composition of CRISPR-Cas12f1 complexes using mass photometry
This webinar explores how the CRISPR-Cas12f1 effector complex recognizes and cleaves DNA. Mass photometry was used to measure the stoichiometry of two miniature Cas12f1 ribonucleoprotein complexes, AsCas12f1 and SpCas12f1 in vitro. The results indicate that the Cas protein forms a binary complex with guide RNA and remains bound when interacting with target DNA, forming a ternary complex. Overall, the results reveal the composition of a compact CRISPR-Cas system and its impact on target recognition and DNA cleavage mechanisms.


BLOG: Studying protein-DNA interactions with mass photometry
In this blog post, we present a recent study that used mass photometry to investigate protein-DNA interactions. We then speak with the paper’s first author, Ananya Acharya, who explains how she and her colleagues used mass photometry to answer unique scientific questions about DNA repair mechanisms and compares it to other techniques.
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