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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Human resource SGLT1-MAP17 complex | |||||||||
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Sample |
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Keywords | Complex / MEMBRANE PROTEIN | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
Authors | Chen L / Zhang XZ | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Sci Adv / Year: 2024Title: Correction of preferred orientation-induced distortion in cryo-electron microscopy maps. Authors: Dongjie Zhu / Weili Cao / Junxi Li / Chunling Wu / Duanfang Cao / Xinzheng Zhang / ![]() Abstract: Reconstruction maps of cryo-electron microscopy (cryo-EM) exhibit distortion when the cryo-EM dataset is incomplete, usually caused by unevenly distributed orientations. Prior efforts had been ...Reconstruction maps of cryo-electron microscopy (cryo-EM) exhibit distortion when the cryo-EM dataset is incomplete, usually caused by unevenly distributed orientations. Prior efforts had been attempted to address this preferred orientation problem using tilt-collection strategy and modifications to grids or to air-water interfaces. However, these approaches often require time-consuming experiments, and the effect was always protein dependent. Here, we developed a procedure containing removing misaligned particles and an iterative reconstruction method based on signal-to-noise ratio of Fourier component to correct this distortion by recovering missing data using a purely computational algorithm. This procedure called signal-to-noise ratio iterative reconstruction method (SIRM) was applied on incomplete datasets of various proteins to fix distortion in cryo-EM maps and to a more isotropic resolution. In addition, SIRM provides a better reference map for further reconstruction refinements, resulting in an improved alignment, which ultimately improves map quality and benefits model building. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_39299.map.gz | 28.7 MB | EMDB map data format | |
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| Header (meta data) | emd-39299-v30.xml emd-39299.xml | 11.9 KB 11.9 KB | Display Display | EMDB header |
| Images | emd_39299.png | 50.4 KB | ||
| Masks | emd_39299_msk_1.map | 30.5 MB | Mask map | |
| Filedesc metadata | emd-39299.cif.gz | 3.8 KB | ||
| Others | emd_39299_half_map_1.map.gz emd_39299_half_map_2.map.gz | 28.2 MB 28.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-39299 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-39299 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_39299.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.167 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_39299_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_39299_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_39299_half_map_2.map | ||||||||||||
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Sample components
-Entire : SGLT1-MAP17
| Entire | Name: SGLT1-MAP17 |
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| Components |
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-Supramolecule #1: SGLT1-MAP17
| Supramolecule | Name: SGLT1-MAP17 / type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 37.6 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.4000000000000001 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: EMDB MAP EMDB ID: |
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| Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.1.1) / Number images used: 280215 |
| Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD |
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About Yorodumi




Keywords
Authors
China, 1 items
Citation






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FIELD EMISSION GUN

