A biomolecular sample is a cornerstone of biochemical, biophysical, and structural analysis. The quality of such sample, especially protein, determines markedly the quality of subsequent measurements. It was suggested  that insufficient sample characterization may cause frequent problems in reproducing the published results. Based on the recommendations by ARBRE and P4EU associations , the basic characteristics of the protein sample (identity, purity, homogeneity, stability) should always be checked for improvement of scientific workflows.
At Biomolecular Interactions and Crystallization Core Facility (CF BIC) at CEITEC, we grant access to the state-of-art instrumentation for biomolecular sample analysis. The purity and homogeneity of the sample are typically assessed by UV/VIS spectrophotometry, analytical size exclusion chromatography (SEC-MALS), dynamic light scattering (DLS), or analytical ultracentrifugation (AUC). The thermal stability of the sample can be measured via differential scanning fluorimetry (nanoDSF), differential scanning calorimetry (DSC), or circular dichroism spectroscopy (CD). CD is also a first-choice method to determine protein and nucleic acid secondary structure. CF BIC ensures maintenance of machines and further develops the methodology, e.g., by designing a novel 48-well buffer screen for optimization of protein conditions . Scientists benefit heavily from the presence of all the techniques in one core laboratory with personal support on site. The combination of various methods allows for detailed analysis of the sample in a short time and spares precious resources of the subsequent high-end analysis.
The further improvement of the services is connected to the facility's involvement in international networks such as ARBRE and Instruct-ERIC. The measurements for academic purposes are also financially supported by Czech Infrastructure for Integrative Structural Biology (CIISB), making the biomolecular characterization affordable to every scientist in the field.
Measurements at Biomolecular Interactions and Crystallization Core Facility are supported by the CIISB project of MEYS CR (LM2018127).