Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cryo-EM structure of mouse heavy-chain apoferritin

ABSTRACT:

SUBMITTER: Sergey Nazarov

PROVIDER: EMPIAR-11866 | biostudies-other |

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Similar Datasets

Cryo-EM structure of mouse heavy-chain apoferritin at 1.62 A

Project description: Not available

| EMPIAR-10216 | biostudies-other

Single particle cryo-EM dataset of mouse heavy chain apoferritin collected on cryoARM300

Project description: Not available

| EMPIAR-10408 | biostudies-other

Cryo-EM structure of 1.51 Angstroms mouse heavy-chain apoferritin in 290 nm gold foil holes (HexAuFoil)

Project description: Not available

| EMPIAR-12240 | biostudies-other

2.7 A cryo-EM structure of vitrified M. musculus H-chain apoferritin from a compact 200 keV cryo-microscope.

Project description:Here we present the structure of mouse H-chain apoferritin at 2.7 Å (FSC = 0.143) solved by single particle cryogenic electron microscopy (cryo-EM) using a 200 kV device, the Thermo Fisher Glacios®. This is a compact, two-lens illumination system with a constant power objective lens, without any energy filters or aberration correctors, often thought of as a "screening cryo-microscope". Coulomb potential maps reveal clear densities for main chain carbonyl oxygens, residue side chains (including alternative conformations) and bound solvent molecules. We used a quasi-crystallographic reciprocal space approach to fit model coordinates to the experimental cryo-EM map. We argue that the advantages offered by (a) the high electronic and mechanical stability of the microscope, (b) the high emission stability and low beam energy spread of the high brightness Field Emission Gun (X-FEG), (c) direct electron detection technology and (d) particle-based Contrast Transfer Function (CTF) refinement have contributed to achieving high resolution. Overall, we show that basic electron optical settings for automated cryo-electron microscopy imaging can be used to determine structures approaching atomic resolution.

| S-EPMC7202636 | biostudies-literature

Single particle cryo-EM dataset of mouse heavy chain apoferritin in plunge-frozen vitrified ice

Project description: Not available

| EMPIAR-11016 | biostudies-other

Single particle cryo-EM dataset of mouse heavy chain apoferritin in laser-melted and revitrified ice

Project description: Not available

| EMPIAR-11017 | biostudies-other

Single particle cryo-EM dataset of mouse heavy chain apoferritin collected on cryoARM300 with beam-image shift of 7 um

Project description: Not available

| EMPIAR-10639 | biostudies-other

Cryo-EM structure of mouse TRPML2 in lipid nanodiscs.

Project description:In mammalians, transient receptor potential mucolipin ion channels (TRPMLs) exhibit variable permeability to cations such as Ca2+, Fe2+, Zn2+, and Na+ and can be activated by the phosphoinositide PI(3,5)P2 in the endolysosomal system. Loss or dysfunction of TRPMLs has been implicated in lysosomal storage disorders, infectious diseases, and metabolic diseases. TRPML2 has recently been identified as a mechanosensitive and hypotonicity-sensitive channel in endolysosomal organelles, which distinguishes it from TRPML1 and TRPML3. However, the molecular and gating mechanism of TRPML2 remains elusive. Here, we present the cryo-EM structure of the full-length mouse TRPML2 in lipid nanodiscs at 3.14 Å resolution. The TRPML2 homotetramer structure at pH 7.4 in the apo state reveals an inactive conformation and some unique features of the extracytosolic/luminal domain and voltage sensor-like domain that have implications for the ion-conducting pathway. This structure enables new comparisons between the different subgroups of TRPML channels with available structures and provides structural insights into the conservation and diversity of TRPML channels. These comparisons have broad implications for understanding a variety of molecular mechanisms of TRPMLs in different pH conditions, including with and without bound agonists and antagonists.

| S-EPMC8808176 | biostudies-literature

Mouse heavy chain apoferritin in plunge-frozen vitreous ice

Project description: Not available

| EMPIAR-11212 | biostudies-other

Mouse heavy chain apoferritin in vitreous ice after plunge-freezing

Project description: Not available

| EMPIAR-11345 | biostudies-other