I am a structural biologist with a specialization in protein crystallography (MX), currently overseeing the FragMAX platform for crystal-based fragment screening at MAX IV Laboratory. My research is focused on structural chemical biology and fragment-based lead development. I am working towards expanding MX accessibility for non-expert users and fostering integration with computational and medicinal chemists, as well as biophysicists, to effectively advance fragment hits into leads.
Tobias Krojer
Lund University
Key Publications
Water Networks as Hydrophobic Recognition Motifs in Proteins.
Angewandte Chemie (International ed. in English), 2025
Structural basis for small molecule binding to the SARS-CoV-2 nsp10-nsp14 ExoN complex.
Nucleic acids research, 2025
Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV.
Journal of synchrotron radiation, 2025
Binding-site purification of actives (B-SPA) enables efficient large-scale progression of fragment hits by combining multi-step array synthesis with HT crystallography.
Angewandte Chemie (International ed. in English), 2025
Accelerating Drug Discovery With High‐Throughput Crystallographic Fragment Screening and Structural Enablement
Applied Research, 2025