We provide all the types of technologies to support your structure studies, including X-ray crystallography, cryo-EM, NMR, MicroED, and SAXS, and we can provide tailored recommendation for your specific needs.

• X-ray Crystallography

— small molecules, high-resolution ligand binding (up to 0.7 Å), fragment screening

• Cryo-EM

— large complexes, membrane proteins, PROTAC ternary complexes (2.0–3.5 Å)

• MicroED

— targets that yield only microcrystals

• NMR

— solution-state dynamics, isotope-labeled proteins (¹⁵N, ¹³C, ²H)

• SAXS (Small-Angle X-ray Scattering)

— particle shape, oligomeric state, and overall structural envelope.

Generally guided by target size and behavior:

• X-ray crystallography

—Smaller, well-behaved, stable domains/proteins/complexes

—High-resolution ligand density needed for SBDD

• Cryo-EM

—Larger or conformationally heterogeneous assemblies, membrane proteins, and complexes, i.e. GPCR-G protein complexes.

We assess this case-by-case and can run parallel tracks for high-priority targets.

At Viva Biotech, AI and structural biology operate as a fully integrated dry-wet lab loop. Structural data from X-ray crystallography and Cryo-EM feeds directly into our proprietary AIDD/CADD platform — covering virtual screening, FEP calculations, and molecular dynamics simulations — to guide compound design. Newly synthesized compounds are then rapidly validated through co-crystal structure determination, enabling faster and more rational lead optimization cycles.

Computational modeling also supports protein engineering by predicting thermostabilizing mutations and identifying flexible or disordered regions to enable more effective construct design. In turn, experimentally determined structures continuously refine AI models, creating a closed-loop workflow that accelerates both protein engineering and drug discovery at Viva.

Viva Biotech's protein crystallography services provide atomic-resolution structures of protein–ligand complexes through co-crystallization and crystal soaking, revealing exact binding modes, key interactions, and allosteric sites that directly inform compound optimization.

With approximately 16,000 crystal structures determined annually and access to 13 synchrotron radiation facilities worldwide, structural insights can be rapidly integrated into AIDD/CADD-guided design and medicinal chemistry cycles.

Yes.

This is a core service area. For low-yield or unstable targets we often combine construct engineering, complex formation with binding partners/fragments to stabilize conformation, and iterative small-scale crystallization/grid trials to conserve material before scaling.