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	Nickel-NTA lipid-monolayer affinity grids allow for high-resolution structure determination by cryo-EM.
Journal, issue, pages	J Struct Biol, Vol. 217, Issue 4, Page 108253, Year 2025
Publish date	Oct 11, 2025
Authors	Aleksandra Skrajna / Clara Lenger / Emily Robinson / Kevin Cannon / Reta Sarsam / Richard G Ouellette / Alberta M Abotsi / Patrick Brennwald / Robert K McGinty / Joshua D Strauss / Richard W Baker /
PubMed Abstract	Grid preparation is a rate-limiting step in determining high-resolution structures by single particle cryo-EM. Particle interaction with the air-water interface often leads to denaturation, ...Grid preparation is a rate-limiting step in determining high-resolution structures by single particle cryo-EM. Particle interaction with the air-water interface often leads to denaturation, aggregation, or a preferred orientation within the ice. Some samples yield insufficient quantities of particles when using traditional grid making techniques and require the use of solid supports that concentrate samples onto the grid. Recent advances in grid-preparation show that affinity grids are promising tools to selectively concentrate proteins while simultaneously protecting samples from the air-water interface. One such technique utilizes lipid monolayers containing a lipid species with an affinity handle. Some of the first affinity grids used a holey carbon layer coated with nickel nitrilotriacetic acid (Ni-NTA) lipid, which allowed for the binding of proteins bearing the commonly used poly-histidine affinity tag. These studies however used complicated protocols and were conducted before the "resolution revolution" of cryo-EM. Here, we provide a straightforward preparation method and systematic analysis of Ni-NTA lipid monolayers as a tool for high-resolution single particle cryo-EM. We found the lipid affinity grids concentrate particles away from the AWI in thin ice (∼30 nm). We determined three structures ranging from 2.4 to 3.0 Å resolution, showing this method is amenable to high-resolution. Furthermore, we determined a 3.1 Å structure of a sub-100 kDa protein without symmetry, demonstrating the utility for a range of biological macromolecules. Lipid monolayers are therefore an easily extendable tool for most systems and help alleviate common problems such as low yield, disruption by the air-water interface, and thicker ice.
External links	J Struct Biol / PubMed:41083086
Methods	EM (single particle)
Resolution	2.41 - 3.1 Å
Structure data	72471 9y45 EMDB-72471, PDB-9y45: His-tagged beta galactosidase (LacZ) on a Ni-NTA lipid monolayer grid Method: EM (single particle) / Resolution: 2.41 Å 72472 9y46 EMDB-72472, PDB-9y46: Human nucleosome structure on Nickel-NTA lipid affinity grid (C2 refinement) Method: EM (single particle) / Resolution: 2.59 Å 72473 9y47 EMDB-72473, PDB-9y47: Human nucleosome structure on Nickel-NTA lipid affinity grid (C1 refinement) Method: EM (single particle) / Resolution: 2.74 Å 72474 9y48 EMDB-72474, PDB-9y48: Sro7 bound to His-Exo84 (1-326) on a Nickel-NTA lipid monolayer Method: EM (single particle) / Resolution: 3.1 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-NA: Unknown entry ChemComp-HOH: WATER
Source	escherichia coli (E. coli) homo sapiens (human) saccharomyces cerevisiae (brewer's yeast)
Keywords	HYDROLASE / beta galactosidase / DNA BINDING PROTEIN / Nucleosome / chromatin / DNA / EXOCYTOSIS / membrane trafficking / vesicle tethering