Inquiry Basket

There is no product in the shopping cart, buy it!

Glyco-engineered Mammalian Cell Expression System Learn More

Knockout and Knockin by Precision Genome Editing Service Learn More

High-throughput Glycan Screening Service Learn More

Glycoprotein Crystal Analysis Services

Glycoprotein Crystal Analysis Services: Transform Complex Targets into Actionable Blueprints!

Are you currently facing challenges in obtaining high-resolution structural data for complex, glycosylated therapeutic targets or difficulty in designing highly selective biologics? Our One-Stop Glycan Crystal & Glycoprotein Crystal Analysis Services help you accelerate lead optimization and define precise therapeutic mechanisms through integrated structural biology, advanced glyco-engineering, and comprehensive biophysical validation. Glycoproteins, characterized by their N- or O-linked glycosylation, are critical cell surface targets in immunology, virology, and oncology. The complexity introduced by these heterogeneous sugar chains is the major challenge in structural biology. Creative Biolab's service leverages the power of X-ray Crystallography to overcome these hurdles, providing atomic models essential for defining function, characterizing ligand binding sites, and establishing the precise structure-activity relationship. This foundation is necessary for rational drug design.

Crystal structure of human cytomegalovirus glycoprotein B. (OA Literature) Fig.1 Crystal structure of viral glycoprotein B.¹

Core Solutions and workflow

Our glycoprotein crystal analysis services provide the atomic-resolution insights. We address the core challenge of membrane-associated and heavily glycosylated targets by delivering high-fidelity structural data, which is essential for rational drug design and mechanism validation. Glycoprotein crystallographic analysis is a multifaceted service that requires specialized expertise in molecular biology, biochemistry, and crystallography to yield high-quality, actionable data. The Creative Biolab workflow is tailored to minimize project risk and maximize the success rate for challenging glycoprotein targets:

High-resolution glycoprotein crystallography services. (Creative Biolabs Original)

The typical timeframe for this service ranges from 12 to 20 weeks, depending heavily on the inherent crystallizability of the target and the difficulty of the phasing challenge. We deliver high-resolution PDB coordinates and structure factors, a detailed structural and mechanistic analysis report.

Specific Glycoprotein Crystal Analysis Services

Creative Biolab provides specialized crystal analysis tailored to the client's objective:

Service	Objective	Key Application
Glycoprotein Crystal based Structural & Functional Analysis Service	Determines the atomic structure of the glycoprotein in its native or stabilized state, establishing the full 3D fold and domain arrangement.	Rational drug and vaccine design; Structure-activity relationship (SAR) studies; Understanding disease mechanism.
Glycoprotein Crystal based Glycosylation Site Analysis Service	Identifies the physical location of N-linked sites and assesses the structural role of surrounding residues and local glycan shielding. It's crucial for engineering antigens and understanding biological functions.	Vaccine design; Bio-similar development.
Glycoprotein Crystal based Glycosylation Type Analysis Service	Utilizes differential expression and Endo H treatment combined with BLI/ITC to correlate glycan type with functional parameters (affinity, kinetics, thermodynamics).	Optimization of expression system for manufacturing; Fab screening for glycan-independent binding.
Crystal based Glycoprotein & Carbohydrate Binding Analysis Service	Achieves co-crystal structures by soaking (small molecules) or co-crystallization (Fab fragments) to visualize the molecular contacts.	Small molecule lead generation; Structure-guided design of glycan mimetics.

Technical Superiority

We specialize in decoding the intricate mechanisms of complex biological systems:

Integrated glyco-engineering

We do not rely solely on mutation. Our capability to express and analyze proteins with complex, high-mannose, and trimmed glycoforms allows us to precisely map the functional role of N-linked glycans on therapeutic binding.

Decoding immune evasion

Our methods are specifically tuned to expose the subtle, yet critical, structural features that viruses use for survival.

Mechanism-based design

We don't just solve structures and interpret their functions. This expertise allows us to identify critical interfaces for therapeutic targeting.

Published Data

This research details the initial crystal structure of the pre-fusion form of the Nipah virus (NiV) Fusion (F) glycoprotein, a molecule critical for initiating host cell membrane merger. The structural analysis first resolved the basic unit of the protein, revealing a tree-like trimer where three identical F subunits interweave around a central axis (as illustrated in the Figure). The most striking discovery, however, was that these F trimers do not exist in isolation but spontaneously assemble into a much larger, ring-shaped hexamer-of-trimers structure, consisting of six trimers total. This higher-order oligomer was confirmed in solution and visualized on virus-like particles (VLPs) using electron tomography, suggesting it is the physiological assembly on the virus surface.

Structure of the Nipah virus-Fusion trimer. (OA Literature) Fig.2 Structure of the NiV-F protein trimer.²

FAQs

Why do I need glycoprotein crystal analysis if I already have binding data from ELISA?

ELISA only confirms binding; our analysis provides the atomic blueprint. Structures differentiate between competitive and allosteric binding, map the exact epitope of your antibody lead, and reveal critical mechanistic insights. This allows for rational, rather than empirical, optimization.

My protein is heavily glycosylated and has failed crystallization attempts before. How does Creative Biolab overcome this?

Glycan heterogeneity is the single biggest barrier. We overcome this by utilizing a tiered approach:
- Targeted construct design (Ig domain truncations);
- Expression in HEK293S cells to yield uniform high-mannose glycans;
- Enzymatic Endo H treatment to leave behind only a single GlcNAc. This dramatically reduces heterogeneity and improves crystal ordering.

I have a dual-activity enzyme like ENPP1. Could you help me design a highly selective drug?

Absolutely. By solving the structure, we can distinguish the active sites and critical interaction interfaces. This atomic-level information is vital for designing drugs that selectively block one function while preserving the other, minimizing adverse effects. Contact us to discuss your selective targeting strategy.

Customer Review

Precision Affinity Data
"Using Creative Biolab's glycoprotein crystal analysis services in our research has significantly improved our ability to resolve low-affinity ligand-glycoprotein interactions using ITC, allowing us to accurately measure affinities in the 200-300μM range that were previously impossible to quantify reliably."- A***an, PhD.

Glycan Focus
"The glycoprotein crystal analysis services offered unparalleled insight into N-linked glycan positioning, confirming that the N286 glycan on our Ig-fold therapeutic target physically restricts Fab binding, a key finding that resolved our antibody development bottleneck. The Endo H treated constructs were instrumental."- E***la, Senior scientist.

Extended Services

To ensure a seamless transition from target identification to lead optimization, Creative Biolab offers complementary services essential for structural biology projects:

Custom protein expression & purification services: High-yield production of challenging mammalian, viral, or bacterial proteins in custom glycoforms.
Biophysical characterization analysis: Standalone kinetics and thermodynamics analysis for rapid ligand screening and binding validation before crystallization efforts.
Advanced Cryo-EM structure determination: For extremely large, flexible complexes, or membrane proteins that are not amenable to crystallization, offering an alternative route to high-resolution data.

Partner with Creative Biolab for Drug Design

Creative Biolabs' platform provides the integrated structural and biophysical rigor to deliver actionable, atomic-resolution data. By partnering with us, you gain access to a platform dedicated to generating these mechanism-defining structures, cutting years off lead optimization, and dramatically improving the probability of developing selective, potent, and safe therapeutic leads. Ready to transform your most challenging targets into atomic blueprints? Please contact us to inquire about more details.

References

Burke, Heidi G., and Ekaterina E. Heldwein. "Crystal structure of the human cytomegalovirus glycoprotein B." PLoS pathogens 11.10 (2015): e1005227. Distributed under an Open Access license CC BY 4.0, without modification. https://doi.org/10.1371/journal.ppat.1005227
Xu, Kai, et al. "Crystal structure of the pre-fusion Nipah virus fusion glycoprotein reveals a novel hexamer-of-trimers assembly." PLoS pathogens 11.12 (2015): e1005322. Distributed under an Open Access license CC0, without modification. https://doi.org/10.1371/journal.ppat.1005322