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
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.
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.
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).
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.