Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Single Particle CryoEM of inactive H2R in complex with Nb6M, NabFab, and anti-fab nanobody

ABSTRACT:

SUBMITTER: Georgios Skiniotis

PROVIDER: EMPIAR-11137 | biostudies-other |

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Similar Datasets

Single Particle CryoEM of inactive SSTR2 bound to Nb6

Project description: Not available

| EMPIAR-11134 | biostudies-other

Single Particle CryoEM of inactive MOR bound to Mb6 and alvimopan

Project description: Not available

| EMPIAR-11135 | biostudies-other

Single Particle CryoEM of inactive hNTSR1 bound to Nb6 and SR antagonist

Project description: Not available

| EMPIAR-11136 | biostudies-other

Fabs enable single particle cryoEM studies of small proteins.

Project description:In spite of its recent achievements, the technique of single particle electron cryomicroscopy (cryoEM) has not been widely used to study proteins smaller than 100 kDa, although it is a highly desirable application of this technique. One fundamental limitation is that images of small proteins embedded in vitreous ice do not contain adequate features for accurate image alignment. We describe a general strategy to overcome this limitation by selecting a fragment antigen binding (Fab) to form a stable and rigid complex with a target protein, thus providing a defined feature for accurate image alignment. Using this approach, we determined a three-dimensional structure of an ?65 kDa protein by single particle cryoEM. Because Fabs can be readily generated against a wide range of proteins by phage display, this approach is generally applicable to study many small proteins by single particle cryoEM.

| S-EPMC3322386 | biostudies-literature

CryoEM single particle dataset for NanR dimer-DNA hetero-complex.

Project description: Not available

| EMPIAR-10836 | biostudies-other

Routine single particle CryoEM sample and grid characterization by tomography.

Project description:Single particle cryo-electron microscopy (cryoEM) is often performed under the assumption that particles are not adsorbed to the air-water interfaces and in thin, vitreous ice. In this study, we performed fiducial-less tomography on over 50 different cryoEM grid/sample preparations to determine the particle distribution within the ice and the overall geometry of the ice in grid holes. Surprisingly, by studying particles in holes in 3D from over 1000 tomograms, we have determined that the vast majority of particles (approximately 90%) are adsorbed to an air-water interface. The implications of this observation are wide-ranging, with potential ramifications regarding protein denaturation, conformational change, and preferred orientation. We also show that fiducial-less cryo-electron tomography on single particle grids may be used to determine ice thickness, optimal single particle collection areas and strategies, particle heterogeneity, and de novo models for template picking and single particle alignment.

| S-EPMC5999397 | biostudies-literature

Single-particle cryoEM data of a ternary KRas(G13D)-SOS complex

Project description: Not available

| EMPIAR-10894 | biostudies-other

Rabbit muscle aldolase single particle cryoEM

Project description: Not available

| EMPIAR-10215 | biostudies-other

Single-particle cryoEM data of yeast Ubr1-Ubc2-Ub-N-degron complex (initiation)

Project description: Not available

| EMPIAR-10886 | biostudies-other

Single-particle cryoEM data of yeast Ubr1-Ub-N-degron complex (pre-elongation)

Project description: Not available