For many targets, no prior structural information or crystal form exists. In these cases, de novo crystallization is the gateway to structural biology. De novo crystallization is notoriously difficult: each protein requires systematic design of construct and broad exploration of conditions. CrystalsFirst overcomes challenges with automation, broad crystallization screening kits, and extensive experience in structure determination.
Comprehensive screening kits: We employ an extensive library of crystallization matrices to maximize coverage across pH, salts, precipitants, and additives.
Automation at scale: Robotic platforms test hundreds of crystallization conditions in parallel, reducing time and increasing reproducibility.
Complex structure determination: Proven experience in solving apo proteins, protein–protein complexes, and protein–ligand assemblies.
Tailored strategies: Flexible approaches depending on protein and ligand characteristics.
Comprehensive screening kits: We employ an extensive library of crystallization matrices to maximize coverage across pH, salts, precipitants, and additives.
Automation at scale: Robotic platforms test hundreds of crystallization conditions in parallel, reducing time and increasing reproducibility.
Complex structure determination: Proven experience in solving apo proteins, protein–protein complexes, and protein–ligand assemblies.
Tailored strategies: Flexible approaches depending on protein and ligand characteristics.
De novo crystallization refers to the first successful crystallization of a protein, protein construct or protein complex when no prior structural data exist. It is essential for unlocking new targets, validating complexes, and enabling downstream structure-based drug design.
We combine broad screening kits with automation, testing hundreds of crystallization conditions systematically. This increases coverage and reproducibility, drastically improving the likelihood of obtaining suitable crystals compared to manual, trial-and-error workflows.
Yes. We have strong experience in solving protein–protein and protein–ligand complexes, adapting crystallization strategies to multimeric systems. This capability is particularly important for structural biology of signaling proteins, enzymes, and drug target assemblies.
Automation enables parallel screening of large condition spaces, minimizes variability, and speeds up the identification of crystallization hits. Robots handle setup and monitoring, while our scientists focus on refinement and optimization.
Clients receive a detailed package including:
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