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Protein Crystallography Service, Gene-to-Structure

Give your structural biology project every chance of success.


Providing successful guaranteed, one stop "Gene-to-Structure" services, from construct design, protein expression, purification and crystallization, finally diffraction screening as well as structure analysis.

Structure 1K project

The NovoPro Structure 1K project is aiming to solve 1000 structures in the next 5 years for. Any protein is welcome to inquiry and join our project, enjoy a special package price and fully risk-free policy.

Gene-to-Structure Complete package 9,998-15,000 USD
Timeline 2-6 months

FREE-If-Fail Guarantee

Meet Protein Date Bank (PDB) requirements

Rfree <0.3, Rwork <0.25


No pre-payment, free-if-fail policy

Top-tier team, overall success rate>60%

Clients hold full intellectual property rights

One-stop and fast service, up to 2 months.

High quality data gather from SSRF, up to 1.0 A resolution

SSRF: The Shanghai Synchrotron Radiation Facility, which operates at 3.5 GeV, the highest energy of any synchrotron other than the Big Three facilities SPring-8 in Hyōgo Prefecture, Japan, ESRF in Grenoble, France and APS at Argonne National labs, United States.


Procedures Timeline Note
1 Gene Synthesis 1-2 Weeks Free construct design and condon optimization
2 Protein Expression and Purification 2-4 Weeks Activity test supported
3 Crystallization 2-8 Weeks Wizard robotics screening, 1500+ conditions
4 Diffraction Data Collection 2-8 Weeks Most advanced Synchrotron facility, SSRF
5 Phasing, Refinement and Analysis 2-3 Weeks Molecular Replacement, Multiple/Single Isomorphous Replacement, or Multiple/Single Anomalous Diffraction
6 PDB Submission and Informatics Analysis 1-2 weeks In-depth analysis of crystal structures on your requirements

How to Start?

For an accurate and efficient communication, please download Structure Request Form and email it back to us. All the target protein will be kept as confidential information. A confidentiality agreement/NDA can also be signed prior to the request form, please contact us if needed.

1. Download and fill Structural Biology Form, send it back to the specified email

2. A project proposal and quote will be provided within 48h from submission of the information form

3. Project agreement

4. Project initiation

5. Data and project report

6. Payment completion

Successful cases

2016.10.10 Signed the project agreement

2016.11.13 Successfully prepared the protein (Purity>95%, denature-refolding)

2016.11.27 Crystal screening and optimization

2016.12.29 Data collection at SSRF

2017.01.04 Structure determination finished, Resolution at 1.7Å, Rwork=0.13, Rfree=0.162


More and more structures are solved at NovoPro…

  • Resolution: 2.0Å; space group: P43212

  • Resolution: 2.19Å; space group: P41

  • Resolution: 1.8Å; space group: P1

  • Resolution: 2.0Å; compound with a small molecular


1. Plasmid for recombinant protein production (optional).

2. Purified recombinant protein for activity test (optional).

3. Project report of experimental details

4. Protein structure and informatics analysis results

Detailed project reports

1. Recombinant protein

  • 1.1 Plasmid:vector map, cloning strategy, sequencing data;
  • 1.2 Protein expression: bacterial strain; expression conditions: temperature, induction time, induction concentration;
  • 1.3 Protein purification: methods and results (gel filtration and SDS-PAGE images);

2. Crystallization

  • 2.1 Protein Crystallization: protein concentration, buff, methods, temperature and other conditions
  • 2.2 Diffraction Data collection:cryo-protectant; X-ray; wavelength; data processing software
  • 2.3 Phasing:methods and software
  • 2.4 Refinement and Analysis:methods and software

3. Structure

  • 3.1 Protein structure .pdb files
  • 3.2 wwPDB X-ray structure validation report
  • 3.3 .sca, .log, .mtz files generated during data analysis

Data collection and refinement statistics will be provided as followings:

Data collection
Wavelength (Å)
Space group
Cell dimensions
a, b, c (Å)
α, β, γ (°)
Resolution (Å)
Rmeas (%)
Rmrgd-F (%)
I / σI
Completeness (%)
Unique reflections
Resolution (Å)
No. reflections
Rwork / Rfree
No. atoms
Favored (%)
Allowed (%)
Outlier (%)
R.m.s. deviations
Bond lengths (Å)
Bond angles (°)