Accelerate your biostructural research

SAXS has a proven track record for reliable determination of macromolecular shape, related parameters and even dynamics and interactions in solutions. So far, these measurements were done at synchrotron facilities or with low throughput laboratory setups requiring large quantities of sample.

With the BioXolver, accelerate your R&D! Get easy access to high quality information on a very large number of samples, using limited quantities of solution, and whenever you need.

Video: BioXolver, Accelerate your biostructural research

Macromolecular shape and dynamics

With the BioXolver, get information on radius of gyration, molecular weight, maximum intra-particle distance, degree of folding, denaturation and low-resolution 3D protein shape.


High throughput measurements and results

From sample to results on 192 samples !

  • Simply place your 2 x 96 well trays on the instrument, press start and walk away.
  • The in–line pipetting robot does automated handling of samples, and the cleaning and drying of the sample cell. No cross contamination of samples. It is fast, reliable & neat.
  • The automated ATSAS package from EMBL in Hamburg analyzes and compiles the results for you.
  • The instrument notifies you via e-mail. Just retrieve your results remotely.

⟩ More samples can be run

⟩ Short sample to sample cycle time

⟩ Results comparable to synchrotron data

⟩ Reproducibility of your measurement is insured

Low sample volume consumption

Tubeless handling of sample volume down to 5 μl

  • Direct injection into measurement cell
  • Automated sample positioning by machine vision

⟩ Save precious sample and money

⟩ Do more with your sample


Directly in your lab

Get information on shape and dynamics of macromolecules in solution right where you are

⟩ No need to wait for synchrotron beamtime

⟩ No sample deterioration during transport

⟩ Reduce your development cycle


Application notes

High throughput protein envelope determination

3D envelopes were determined from an automated sequence of measurements including 3 different proteins with low volume and dilute solutions.

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Thorough investigation of oligomers during protein fibrillation

The transient nature of aggregates during the fibrillation process of α-synuclein is highlighted with in-house SAXS experiments using the BioXolver.

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Protein-protein interactions – from in vivo functionality to pharmaceutics and food science

Salt concentration and pH impact were studied on lysozyme and BSA systems respectively by investigating various parameters (osmotic second virial coefficient, folding state and 3D shape).

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In-lab SEC-SAXS for structural investigation of complex samples

SAXS data and 3D envelopes of small and large protein species are obtained through in-line gel filtration.

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