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export data from discoveryMP
Hi,
I would like to export the mass data and the counts to re-fit the data using different software. How can I do that? Thank you very much,
My
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Filter settings
Hi,
we recently got the hint that we could analyze our MP spectra with all the filters turned right down, to let in as much noise as possible (in both binding and unbinding). I saw that this was mentioned in the manual for the OneMP but we have a TwoMP with Discover MP v2024 R1. Is there a way to access this options in our setup too? Additionally, I found under preferences an advanced mode which requires a password that we are not aware of. Is there a way to get into the advanced mode?
Thank you for your help!
Axel
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Positive and negative peaks for the same sample
Why does the same sample give positive and negative peaks (see the attachment)? Does this result indicate binding and unbinding?
Thilini-Case Western Reserve
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Nanoparticles – biological entity interactions
Is it possible to study interactions of synthetic nanoparticles with biological entities (e.g. formation of a protein corona around polystyrene nanoparticles) by mass photometry? I suppose calibration would be an issue, and perhaps there would be some other difficulties.
Thank you very much,
Jitka
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Macro mass photometry - bacterial cells
Is it likely (currently or in future) that macro mass photometry would be used to characterize mycoplasma (or other bacteria) in some way? Some mycoplasma cells are around the upper size limit of KaritroMP but I understand that they are rather complex in comparison to viruses or biomolecules.
Thank you,
Jitka
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Laser wavelength used in the (macro) mass photometers?
What is the laser wavelength used in the mass photometry instruments including KaritroMP? Is the wavelength the same in all your instruments?
Thank you,
Jitka
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Is there a way to subtract buffer background?
I'm trying to look at oligomerization for a 37kDa protein, and there is a lot of overlap between the monomer and the background from the buffer. Is there a way to subtract the background from the monomer peak?
Thanks.
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Team Refeyn
Jul 21, 2025
Hi Felicity,
No, there is no way to do that. If they are using MassGlassUC we would recommend they hand clean the slides for any protein smaller than 50 kDa (protocol attached), and that they make sure they use a buffer without noise. They could use 1x buffer for cell culture grade, or if the buffer is prepared from tablets or concentrates they could mix it for a long time at a temperature higher than room temperature to favour a better dissolution of all components.
Best Regards,
Team Refeyn
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Directions for using/storing MassFerence P1 Calibrant
Is there any documentation for this?
I read on the vial that the calibrant is 500X and a volume of 50 uL. Can I prepare 20 uL aliquots at 2X and store them at -20 to avoid repeated freeze/thaw cycles?
Any information is welcome.
Thanks,
Ryan
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Team Refeyn
Mar 03, 2025
Hi Ryan,
We have not tested “20 uL aliquots at 2X” and hence unable to comment on the product stability at such dilutions. But what we can say is for best results, aliquot 10 x 5 µL upon first thaw and store to avoid repeated freeze/thaw cycles.
Best,
Team Refeyn
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MassFluidix limit of detection
I had a question regarding the limit of detection using the MassFludix device. I read that the lower limit is 50 kDa. My protein of interest is ~35 kDa based on MP measurements and SEC analysis. If I were to run this protein on the MassFluidix what would happen? I noticed that running a PBS blank produces a peak that was called ~54 kDa, close to the limit of detection. For a protein below the 50 kDa cutoff would it look similar to a PBS run?
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Hi My Le,
Yes, if you have version v2025 R1 (or later) of the software installed you can go ahead and update. Please contact support@refeyn.com if you have any further questions or issues.
Best regards,
Team Refeyn