1 - MacroDSF analytical instrument


Value proposition:

Recent technological advances in X-ray and EM technology have often made the specimen itself become the limiting factor. MacroDSF guides you to more stable proteins and thus improves specimen quality. The machine with its patented algorithm helps you find the ideal conditions - e.g. optimal protein concentration, pH value, salt, type of buffer, type of stabilizing additive - to stabilize your protein. This knowledge can dramatically improve your purification results and allows high quality structure determination, e.g. protein might regularly crystallize after MacroDSF improvement.



Only technology that can cope with multi-domain proteins due to unique biophysical algorithm


Success story (example):

Stability optimization of human 20S proteasome, leading to an unprecedented resolution of 1.8A and a 10x times higher specific activity than anything reported before


Answers to FAQ / Caveats:

  • MacroDSF is not applicable to membrane proteins​ as the micelles distort the signal
  • Buffer improvement does not always mean to get better images. There are many other parameters that can destabilize or even destroy a protein complex. Thus, buffer optimization is not a panacea but one of many levers to be checked; it can be a limiting condition - or not.
  • Yes, there are cases where Thermofluor/DSF yields similar results as ProteoPlex MacroDSF. But, as a matter of fact, Tm is a physically wrong criterion for complexes which might - coincidentally - be "right". In general, the results from MacroDSF and Thermofluor/DSF converge with increasing protein optimization, i.e. results of both methods agree for complexes that require no further optimization and are already present in a stabilized form. In the early stages of a project, there should hardly be any overlap between the two methods and that is where ProteoPlex can be a real asset, as shown in Fig. 1.

Fig. 1: Comparison to conventional data interpretation. Comparison of melting-curve evaluation by ProteoPlex and conventional DSF. Results obtained by both methods perfectly agree (green) only for complexes that require no further optimization and are already present in a stabilized form. In early stages of a project, there is no overlap between DSF and ProteoPlex results.


Flyer MacroDSF
20170113 ProteoPlex flyer v01.pdf
PDF-Dokument [621.2 KB]


Suggested further reading:

Chari, A.; Haselbach, D.; Kirves, J. M.; Ohmer, J.; Paknia, E.; Fischer, N.; Ganichkin, O.; Moller, V.; Frye, J. J.; Petzold, G. et al.: ProteoPlex: Stability optimization of macromolecular complexes by sparse-matrix screening of chemical space. Nature Methods 12 (9), S. 859-865 (2015)


Download: http://www.nature.com/nmeth/journal/v12/n9/full/nmeth.3493.html


Business model:

Sell machine / software



Intl. patent, exclusive license from Max-Planck






MacroDSF presentation: