300+
Structures Solved
1.0 Å
Best Resolution
1 Month
Fastest Turnaround
1–3
Months Gene-to-Structure
5
Global Beamlines
Service Overview
The Gold Standard for High-Resolution Protein Structure Determination
X-ray crystallography remains the primary technique for determining protein and macromolecular complex structures at atomic resolution. By diffracting X-rays through protein crystals and analyzing the resulting diffraction patterns, electron density maps are computed from which complete atomic models are built and refined to Ångström-level precision.
iCDMO's crystallography service covers the complete pipeline — from gene-to-crystal protein production, high-throughput crystallization screening with 2,000+ conditions, and synchrotron data collection at Diamond, ESRF, APS, SSRF, and Spring 8, through structure determination, PDB deposition, and biological interpretation — all under one roof.
Suitable For
Small to medium-sized soluble proteins (MW < 100 kDa preferred)
Proteins forming well-diffracting crystals (enzymes, kinases, receptors)
Membrane proteins via detergent or lipidic cubic phase (LCP) crystallization
Protein–ligand, protein–inhibitor, and protein–cofactor co-crystals
Fragment-based drug discovery (FBDD) soaking campaigns
Protein complexes and multi-subunit assemblies that can be crystallized
Stable proteins without major conformational flexibility in the crystal
Crystallization Process
Three-Phase Crystallization Screening
Our systematic three-phase approach — from initial high-throughput screening to crystal identification — maximizes success even for challenging targets.
Methods
Crystallization Techniques
Vapor diffusion is the core technique in our crystallization platform, implemented via sitting-drop and hanging-drop methods.
Service Workflow
From Gene to PDB Deposition
A systematic, quality-controlled pipeline that has delivered 300+ high-resolution structures across all target classes.
01
01
Crystallization-Grade Protein Production
Gene construct design & codon optimization for target host
Protein expression: E. coli, baculovirus/Sf9, or mammalian HEK-293
Multi-step purification: IMAC affinity, ion exchange, SEC polishing
QC: SDS-PAGE, DLS (polydispersity), SEC-MALS (MW), thermal shift (Tm)
02
02
Initial 96-Well Crystallization Screening
High-throughput sitting-drop and hanging-drop vapor diffusion
2,000+ commercially formulated conditions screened in parallel
Nanoliter dispensing: Mosquito LCP and Crystal Gryphon robots
UV CrysCam fluorescence imaging to identify protein vs. salt crystals
03
03
Optimization of Crystallization Hits
Fine-tuning of pH, precipitant concentration, additive, and temperature
Seeding: streak seeding, micro-seed matrix screening (MMS)
Detergent and lipid additive screens for membrane protein co-crystals
Ligand co-crystallization and soaking with inhibitors or cofactors
04
04
Synchrotron Radiation Data Collection
Remote beamline access: SSRF, Diamond (I03/I04), ESRF (ID23), APS, Spring 8
In-house Cu Kα rotating anode for preliminary space-group screening
Cryo-loop mounting, flash-cooling in liquid nitrogen, cryo-stream data collection
Multi-wavelength anomalous diffraction (MAD) at tunable beamlines for de novo phasing
05
05
Structure Determination, Modeling & Refinement
Data processing & scaling: HKL3000, XDS, AIMLESS; space group determination
Phasing: Molecular Replacement (Phaser), SAD/MAD (SHELX), MIR (SOLVE)
Model building: Coot, ISOLDE; iterative refinement: REFMAC5, PHENIX.refine, BUSTER
Validation: MolProbity, Rfree, Ramachandran; PDB deposition & manuscript figures
From Crystal to Atomic Structure
The complete X-ray crystallography pipeline — from growing the crystal to depositing refined atomic coordinates in the PDB.
Why Choose iCDMO
Service Advantages
Highest Resolution
X-ray crystallography routinely achieves 1.0–2.5 Å resolution — sufficient to resolve individual atoms, water molecules, and bound ligand geometry with full precision.
Co-Crystal with Ligands
Industry-standard for structure-based drug design: visualize how inhibitors, fragments, and drug candidates bind within the active site at atomic detail.
Synchrotron Access
Established access to major global beamlines (Diamond, ESRF, APS, SSRF, Spring 8) ensures highest-quality diffraction data for even weakly diffracting crystals.
300+ In-House Structures
Our structure gallery of 300+ solved proteins provides search models for rapid Molecular Replacement phasing, cutting time-to-structure for related targets.
PDB-Grade Validation
All structures validated to PDB wwPDB criteria — Rfree, Ramachandran, MolProbity scores — and deposited with full structure factor files for open access.
FBDD Campaign Support
Fragment soaking campaigns against pre-formed crystals: screen 500–1,000 fragments crystallographically to identify novel chemical starting points for lead discovery.
Case Studies
Representative Solved Structures
Services Included
Frequently Asked Questions
Note: Timelines are estimates for well-behaved samples. Challenging targets or low-symmetry crystal forms may require additional optimization cycles. Contact us for a free feasibility assessment before project initiation.
Free Feasibility Assessment
Share your target details and our crystallographers will assess feasibility and recommend the optimal crystallization strategy within 24 hours.
Contact Us Online ConsultationStandard Deliverables
✓Atomic coordinate PDB file
✓Structure factor MTZ file
✓MolProbity validation report
✓Detailed refinement statistics
✓Publication-quality PyMOL figures
✓Biological interpretation report
✓PDB deposition assistance
✓Manuscript preparation support