The Interdisciplinary Nanoscience Center at Aarhus University: New Assistant Professor Joins iNANO

Max earned his PhD in 2018 from the Biozentrum at the University of Basel, and has since conducted postdoctoral research at Stockholm University, UCLA, and HHMI. In 2024, he was awarded a DKK 10 million Novo Nordisk Foundation Hallas-Møller Emerging Investigator grant to support his work on crystalline pathologies.

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Max’s research aims to develop new approaches for in situ electron crystallography that integrate MicroED and FIB/SEM technologies, enabling scientists to study functional materials and naturally occurring crystalline proteins in their native environments.

A major aspect of his work is involved with expanding the current toolbox of diffraction methods, utilizing automated and serial data collection strategies that leverage MicroED and 4D-STEM. High-throughput structural analysis is also key to understanding nanocrystalline samples in materials science and chemistry, enabling rapid structure determination at atomic resolution (Figure 1).

Figure 1. A typical workflow involved in electron crystallography. Nanocrystals of L-Tyrosine are directly deposited onto a standard electron microscopy grid covered with a thin carbon film. Grid squares with suitable crystals are identified from a full grid atlas collected at low magnification. At higher magnification, individual nanocrystals are selected for data collection. Continuous rotation MicroED data are recorded in movie mode using a parallel electron beam of 2 micron diameter. Data show diffraction spots that extend to even beyond the edge of the camera at 0.54 Å resolution. At atomic resolution, the structure is solved using direct methods. Scale bars are 20 μm and 500 nm, respectively. The electrostatic potential map is shown as blue mesh contoured at 1.2σ. Carbon atoms are black, oxygen red, nitrogen blue, and hydrogens white. Data were collected on the Titan Krios G3i at the EMBION cryo-EM facility at iNANO.

Max recently published a study in Nature Communications from his work at HHMI and UCLA, demonstrating how removing inelastically scattered electrons using energy filtering significantly improves the signal-to-noise ratio in MicroED experiments (Figure 2). Reducing background noise enabled recovering more structural information at atomic resolution from proteinase K crystals, allowing researchers to visualize fine structural details and gain deeper insights into protein structure and function.

Read the full paper in Nature Communications

Figure 2. Energy filtering removes inelastically scattered electrons and substantially improves MicroED data quality and resolution, reducing background noise and sharpening diffraction spots. Data were recorded from 300 nm thin crystalline lamellae of proteinase K, a widely used enzyme for protein degradation, using a fluence of 0.84 e-/Å2 for each diffraction pattern (equivalent to a dose of approximately 3.1 MGy). The edge of the detector is at 1.0 Å resolution.

Contact

Assistant Professor Max Theo Ben Clabbers
Aarhus University
Interdisciplinary Nanoscience Center (iNANO)
Department of Molecular Biology and Genetics
E-mail: mtbc@inano.au.dk