6S2N

Hen egg-white lysozyme by serial electron diffraction

Summary for 6S2N

• Entry DOI: 10.2210/pdb6s2n/pdb
• EMDB information: 10090
• Descriptor: Lysozyme C (2 entities in total)
• Functional Keywords: lysozyme, hewl, serial crystallography, hydrolase
• Biological source: Gallus gallus (Chicken)
• Total number of polymer chains: 1
• Total formula weight: 14331.16

Authors

Buecker, R.,Mehrabi, P.,Schulz, E.C.,Hogan-Lamarre, P. (deposition date: 2019-06-21, release date: 2020-04-29, Last modification date: 2024-10-23)

Primary citation

Bucker, R.,Hogan-Lamarre, P.,Mehrabi, P.,Schulz, E.C.,Bultema, L.A.,Gevorkov, Y.,Brehm, W.,Yefanov, O.,Oberthur, D.,Kassier, G.H.,Dwayne Miller, R.J.
Serial protein crystallography in an electron microscope.
Nat Commun, 11:996-996, 2020

PubMed Abstract: Serial X-ray crystallography at free-electron lasers allows to solve biomolecular structures from sub-micron-sized crystals. However, beam time at these facilities is scarce, and involved sample delivery techniques are required. On the other hand, rotation electron diffraction (MicroED) has shown great potential as an alternative means for protein nano-crystallography. Here, we present a method for serial electron diffraction of protein nanocrystals combining the benefits of both approaches. In a scanning transmission electron microscope, crystals randomly dispersed on a sample grid are automatically mapped, and a diffraction pattern at fixed orientation is recorded from each at a high acquisition rate. Dose fractionation ensures minimal radiation damage effects. We demonstrate the method by solving the structure of granulovirus occlusion bodies and lysozyme to resolutions of 1.55 Å and 1.80 Å, respectively. Our method promises to provide rapid structure determination for many classes of materials with minimal sample consumption, using readily available instrumentation.

PubMed: 32081905
DOI: 10.1038/s41467-020-14793-0

Experimental method

ELECTRON CRYSTALLOGRAPHY (1.8 Å)