SAMPLE PREPARATION FOR
Protein Production & Purification

Protein samples prepared with the structural biology question in mind.

Reliable protein samples for the next structural decision.

Successful structural biology begins with high-quality protein samples. Protein expression level, purity, homogeneity, stability, and complex formation all influence what can be achieved by X-ray crystallography, cryo-EM, mass photometry, or downstream biochemical analysis.

At BIMOVIS, protein production and purification are not treated as isolated technical steps. We look at the target, construct design, sample history, and intended structural biology workflow together, so that the preparation strategy fits the scientific question.

Our capabilities include recombinant protein expression, purification, buffer optimization, stability assessment, alternative membrane protein environments, and preparation of protein complexes. The goal is to generate material that is not only pure, but suitable for the next experimental decision.

Better Samples, Clearer Data, and More Reliable Structural Insights.

Protein production and purification define the starting point for many structural biology projects. A sample may look acceptable by concentration alone, but still contain aggregation, degradation, mixed oligomeric states, or unstable complexes that limit downstream analysis.

By assessing and optimizing the sample early, many project risks become visible before larger experimental efforts begin. This is especially important for difficult targets, multi-component complexes, membrane-associated proteins, and projects where several constructs or conditions need to be compared.

At BIMOVIS, we integrate protein production and purification with downstream structural biology workflows to assess whether a sample is ready for crystallization, cryo-EM, negative stain EM, mass photometry, or further optimization.

Recombinant protein expression and construct-level considerations
Protein purification for structural biology workflows
Assessment of purity, homogeneity, stability and aggregation
Preparation and evaluation of protein complexes
Buffer and condition optimization for downstream analysis
Sample strategy for crystallography, cryo-EM and complementary methods

How we work.

Project scoping & target review

We discuss the target, available sequence or construct information, previous expression data, and the intended downstream application.

Construct and expression strategy

We define a practical expression approach based on the molecule, required material, and structural biology workflow.

Protein expression

Protein is produced using a suitable recombinant expression setup, with attention to yield, solubility, and sample integrity.

Purification & optimization

Purification is adapted to the target and project goal, with optimization of conditions where needed to improve sample quality.

Sample quality assessment

We assess purity, concentration, homogeneity, stability and, where relevant, complex formation or oligomeric state.

Preparation for downstream work

The final sample strategy is aligned with the next step, such as crystallization, cryo-EM, negative stain EM, mass photometry, or biochemical analysis.

Project scoping & target review

We discuss the target, available sequence or construct information, previous expression data and the intended downstream application.

Construct and expression strategy

We define a practical expression approach based on the molecule, required material and structural biology workflow.

Protein expression

Protein is produced using a suitable recombinant expression setup, with attention to yield, solubility and sample integrity.

Purification & optimization

Purification is adapted to the target and project goal, with optimization of conditions where needed to improve sample quality.

Sample quality assessment

We assess purity, concentration, homogeneity, stability and, where relevant, complex formation or oligomeric state.

Preparation for downstream work

The final sample strategy is aligned with the next step, such as crystallization, cryo-EM, negative stain EM, mass photometry or biochemical analysis.

Where this service applies.

Protein production and purification support projects where sample quality, stability and molecular behavior are central to the structural biology workflow.

Structure-Based Drug Design

Early evaluation of target complexes or structural biology readiness before committing to high-resolution workflows.

AI Structure Model Validation

Experimental context for whether the expected complex, assembly or particle state is present in the sample.

Antibody Epitope Mapping

Screening of antibody-antigen complexes before more detailed structural analysis by cryo-EM or crystallography.

PROTAC Design

Production of target proteins or complex components needed for structural and computational degrader workflows.

Protein Engineering

Insight into complex architecture, domain organization and structural features that can guide protein design or optimization.

Protein questions.

When should I use protein production and purification services?

Protein production and purification services are useful when you need high-quality protein material for structural biology, biophysical characterization, or drug discovery. BIMOVIS can support projects starting from a gene sequence, existing construct, or challenging protein target, with sample preparation tailored to the intended downstream application.

What factors determine whether a protein sample is suitable for structural biology?

Successful structural studies depend on more than protein purity alone. Expression level, homogeneity, stability, aggregation, oligomeric state, and complex formation all influence experimental outcomes. During protein sample preparation, BIMOVIS evaluates these characteristics to determine whether additional optimization is needed before structural analysis.

Can BIMOVIS support difficult or challenging protein targets?

Yes. BIMOVIS supports challenging targets including membrane proteins, multi-protein complexes, engineered variants, and proteins with limited expression or stability. Expression, purification, and sample preparation strategies can be adapted to the target and intended structural workflow.

What happens if my protein sample is not suitable for structural studies?

If a sample does not meet the required quality criteria, BIMOVIS works with you to identify the underlying challenges. Depending on the project, this may include optimizing expression conditions, refining purification methods, adjusting buffer composition, improving protein stability, or evaluating alternative constructs before proceeding with structural analysis.

Extend your project.

X-ray Crystallography

Atomic-level structure determination for suitable proteins, complexes and protein-ligand systems.

Cryo-Electron Microscopy (Cryo-EM)

Structural analysis of larger complexes, membrane proteins and dynamic molecular assemblies.

Mass Photometry

Solution-based assessment of molecular mass, oligomeric state, complex formation and sample heterogeneity.

Go deeper in our Knowledge Hub.

Guides, protocols, and reference materials to support your structural biology projects — free to access.

SAMPLE PREPARATION FOR Protein Production & Purification