Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Sub-3 Å resolution protein structure determination by single-particle cryo-EM at 100 keV.
Journal, issue, pages	Structure, Vol. 33, Issue 10, Page 1717-11727.e4, Year 2025
Publish date	Oct 2, 2025
Authors	Dimple Karia / Adrian F Koh / Wen Yang / Victoria I Cushing / Benjamin Basanta / Daniel B Mihaylov / Sagar Khavnekar / Ondřej Vyroubal / Miloš Malínský / Ondřej Sháněl / Vojtěch Doležal / Jürgen Plitzko / Lingbo Yu / Gabriel C Lander / A Radu Aricescu / Basil J Greber / Abhay Kotecha /
PubMed Abstract	Cryoelectron microscopy (cryo-EM) has transformed structural biology by providing high-resolution insights into biological macromolecules. We report sub-3 Å resolution structures using the 100 keV ...Cryoelectron microscopy (cryo-EM) has transformed structural biology by providing high-resolution insights into biological macromolecules. We report sub-3 Å resolution structures using the 100 keV Tundra cryo-TEM, equipped with the Falcon C direct electron detector (DED). This system combines advanced optics, extreme-brightness field emission gun (XFEG), and SP-TWIN lens to enhance coherence and resolution. The semi-automated loader reduced contamination and drift, enabling extended data collection, while the high detective quantum efficiency (DQE) of Falcon C improved signal-to-noise ratio. We validated performance by determining structures of biological samples, including apoferritin (2.1 Å), T20S proteasome (2.7 Å), GABA receptor (2.8 Å), hemoglobin (5.0 Å), transthyretin (3.5 Å), and AAV9 capsid (2.8 Å), spanning 50 kDa-3.9 MDa. This work highlights the potential of 100 keV transmission electron microscopes (TEMs) to make cryo-EM more accessible. It sets a precedent for using lower voltage TEMs not only for screening, but also for high-resolution protein structure determination.
External links	Structure / PubMed:40744008 / PubMed Central
Methods	EM (single particle)
Resolution	2.1 - 5.0 Å
Structure data	EMDB-13769: CryoEM structure of Apoferritin at 2.6A from Tundra, 100kV microscope Method: EM (single particle) / Resolution: 2.6 Å EMDB-13816: CryoEM structure of GABA(A)R-beta3 homopentamer at 3.4A from Tundra, 100kV microscope Method: EM (single particle) / Resolution: 3.4 Å EMDB-14249: CryoEM structure of T20S proteasome at 3A from Tundra, 100kV microscope Method: EM (single particle) / Resolution: 3.0 Å EMDB-51463: ApoF at 2.2A resolution imaged at 0.55A/pixel on Falcon C Method: EM (single particle) / Resolution: 2.2 Å EMDB-51481: Apoferritin at 2.1A from Falcon C imaged at 0.7Apix Method: EM (single particle) / Resolution: 2.1 Å EMDB-51483: Apoferritin at 2.2A from Falcon C imaged at 0.9Apix Method: EM (single particle) / Resolution: 2.2 Å EMDB-51487: T20S Proteosome at 2.7A from Falcon C imaged at 0.7Apix Method: EM (single particle) / Resolution: 2.7 Å EMDB-51503: T20S Proteosome at 2.9A from Falcon C imaged at 0.9Apix Method: EM (single particle) / Resolution: 2.9 Å EMDB-51506: GABAA receptor at 2.8A from Falcon C imaged at 0.7Apix Method: EM (single particle) / Resolution: 2.8 Å EMDB-51508: GABAA receptor at 2.8A from Falcon C imaged at 0.9Apix Method: EM (single particle) / Resolution: 3.2 Å EMDB-51511: Rabbit muscle aldolase at 3A resolution imaged at 0.55A/pix Method: EM (single particle) / Resolution: 3.0 Å EMDB-51512: Rabbit muscle aldolase at 2.8A imaged at 0.7Apix Method: EM (single particle) / Resolution: 2.8 Å EMDB-51519: CAK complex at 4A imaged on Falcon C Method: EM (single particle) / Resolution: 4.0 Å EMDB-51525: Human Haemoglobin at 5A imaged on Falcon C Method: EM (single particle) / Resolution: 5.0 Å EMDB-51526: Human Transthyretin at 3.5A imaged on Falcon C Method: EM (single particle) / Resolution: 3.5 Å EMDB-51540: Adeno-associated Virus 9 at 2.8A imaged on Falcon C Method: EM (single particle) / Resolution: 2.8 Å
Source	Escherichia coli (E. coli) HEK 293S cells (E. coli) Thermoplasma acidophilum (acidophilic) Mus musculus (house mouse) Homo sapiens (human) Oryctolagus cuniculus (rabbit)