9HKI

Plunge-frozen beta-galactosidase

Summary for 9HKI

• Entry DOI: 10.2210/pdb9hki/pdb
• EMDB information: 52230
• Descriptor: Beta-galactosidase, MAGNESIUM ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: glycoside hydrolase, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 465245.20

Authors

Barrass, S.V.,Esser, T.K.,Mowry, N.J.,Eriksson, L.,Hruby, J.,Seeley, L.T.,Drabbels, M.,Baker, L.A.,Rauschenbach, S.,Lorenz, U.J. (deposition date: 2024-12-03, release date: 2025-12-17, Last modification date: 2026-10-28)

Primary citation

Barrass, S.V.,Esser, T.K.,Mowry, N.J.,Eriksson, L.,Wenz, J.,Seeley, L.T.,Curtis, W.A.,Baker, L.A.,Drabbels, M.,Rauschenbach, S.,Lorenz, U.J.
Cryo-EM sample preparation with soft-landing and laser flash melting.
Nat Commun, 17:-, 2026

PubMed Abstract: The preparation of cryo-EM samples by soft-landing mass spectrometry promises to significantly simplify sample optimization, which has remained an important bottleneck in single-particle cryo-electron microscopy (cryo‑EM). However, only compacted configurations are observed after soft-landing since the proteins are dehydrated in the process. Here, we deposit a layer of amorphous ice onto the sample and briefly flash melt it to rehydrate the soft-landed proteins. Melting with a 30 µs laser pulse creates a broad ensemble of partially rehydrated structures. However, a subset of particles returns to a configuration close to the native state. This allows us to propose strategies to fully rehydrate the entire ensemble and brings routine sample preparation by soft-landing mass spectrometry within reach.

PubMed: 42881156
DOI: 10.1038/s41467-026-77723-6

Experimental method

ELECTRON MICROSCOPY (1.9 Å)