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ATEM
Cryo-EM platform

Taking cryo-EM the extra step

Protein structures, AAV, viral particles, lipid nanoparticles, and dynamics—we offer a comprehensive arrangement of solutions spanning analytics and 3D structure determination. We harness the potential of industrial Cryo-EM technology through a combination of expert biochemistry and state-of-the-art hardware. 

AT THE FOREFRONT OF
INDUSTRIAL CRYO-EM TECHNOLOGY

LET'S DISCUSS YOUR PROJECT

We focus on cryo-EM

We deliver distinct dynamic conditions of protein targets with an efficient data recording and processing platform. Besides using standardized methods, we aim to take cryo-EM a step forward. We pave our own path and work on creating novel solutions with AI for enhanced understanding of protein dynamics.

Biochemistry

Proprietary software

The science behind

single-particle cryo-EM

Quality screening

Your cryo-EM structure starts with sample preparation. Once we receive your purified sample (1), we quickly process it with a negative stain analysis. This allows us to check sample quality and get back to you with a report on how the samples look in the microscope.

Cryo-EM

After the sample’s quality control, we proceed to prepare the grids (2). We do this by adding a small amount (only a few µl) of your sample to a cryo-grid and blotting it to achieve a thin layer of liquid. The grid is then vitrified in liquid ethane (3) so rapidly that the sample retains its native state without forming ice crystals.

Processing

Our specialists process the data quality and start collecting images (4). These images are analyzed and processed according to our standardized methods (5). We start 3D reconstruction and create a final structure from the density map (6). In the end, you receive an extensive report with the 3D structure as a PDB file.

The Rise of Cryo-EM

Join the resolution revolution

Since the 1950s, scientists laid the foundations for visualizing protein structures. They gazed upon the unseen and unlocked the hidden nature of protein biology by combining innovative machinery together with human ingenuity. The first protein structure was obtained using x-ray crystallography, a method that relies on sending x-ray beams through proteins in a crystalized lattice. This method has dominated the structural biology field until recently.

Cryogenic electron microscopy (cryo-EM) uses beams of electrons to highlight proteins in a variety of orientations. One can think of it like a projector that shines on an object, creating contrast in the light and showing the object’s shape. With thousands or millions of different orientations, scientists can combine and reconstruct the shapes in a single, 3-dimensional view. While being a substantial method, cryo-EM fought to provide the same high-resolution structures of x-ray crystallography due to hardware limitations. In recent years, this has changed, with advances in cryo-EM leading to the so-called “resolution revolution”.

The resolution revolution shaped cryo-EM into a powerful method that now competes closely with x-ray crystallography when it comes to resolution. It provides certain benefits over x-ray crystallography by requiring much lower sample amounts and targeting challenging projects such as complexes and membrane proteins, with higher reliability. Since protein samples are vitrified instead of crystallized, it allows a look into how the protein behaves in solution. In other words—we can see the natural dynamics that govern protein function.

One method – multiple aspects

Cryo-EM takes on challenges with ease. Membrane proteins, large complexes, and flexible proteins—all are applicable candidates. With the natural, soluble state of the protein sample, it is possible to visualize and determine the binding of ligands and antibodies. Proteins are often flexible by nature, transporting chemicals into cells or responding to cascades that trigger complicated events. With cryo-EM, these flexible traits can be determined. Important mutations can be discerned and compared to their wild-type counterpart, providing atomic details of how diseases work. Antibodies can be developed with high certainty by locating their binding domains and epitopes on the antigen.

Cryo-EM and transmission electron microscopy (TEM) are not only used to discern structural data. Analytics combines visual and quantitative data by analyzing lipid nanoparticles (LNP) and adeno-associated virus (AAV) delivery systems. We test cellular samples with TEM for viral particle analysis, ensuring certainty and safety before drug release testing. TEM offers a unique addition to other methods by visualizing samples and determining the quality by ruling out contamination and unfavorable morphology – all in one single analysis.

We at ATEM focus entirely on electron microscopy. Our scientific team consists of specialists that together combine decades of work in protein biochemistry, cryo-EM, and data engineering. Our passion is reflected in our results, and we dedicate ourselves to reliability and transparency in order to take on the challenges of drug design and scientific discovery.

Cryo-EM

Sample quantity: low / medium
Protein / Complex size: small - very large
Native state: yes
Dynamics visualization: yes
Need for crystallization: no

X-Ray Crystallography

Sample quantity: high
Protein / Complex size: high
Native state: no
Dynamics visualization: no
Need for crystallization: no

NMR

Sample quantity: high
Protein / Complex size: small
Native state: yes
Dynamics visualization: yes
Need for crystallization: yes

Cryo-EM

X-Ray Crys­tall­ography

NMR

Sample amount
low / medium
high
high
Protein/Complex size
>50 kDa
small-large
<50 kDa
Native state
yes
no
yes
Protein dynamics
yes
no
yes
Need for crystallization
no
yes
no