+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-7528 | |||||||||
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Title | Rabbit muscle aldolase at 2.8 A (17dec27a- 1st 382 img) | |||||||||
Map data | Rabbit muscle aldolase 17dec27a, 1st 382 images. 2.8A with 87K particles in 11.9 hours. | |||||||||
Sample |
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Biological species | Oryctolagus cuniculus (rabbit) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.8 Å | |||||||||
Authors | Kim LY / Rice WJ / Eng ET / Kopylov M / Cheng A / Raczkowski AM / Jordan KJ / Bobe D / Potter CS / Carragher B | |||||||||
Citation | Journal: Front Mol Biosci / Year: 2018 Title: Benchmarking cryo-EM Single Particle Analysis Workflow. Authors: Laura Y Kim / William J Rice / Edward T Eng / Mykhailo Kopylov / Anchi Cheng / Ashleigh M Raczkowski / Kelsey D Jordan / Daija Bobe / Clinton S Potter / Bridget Carragher / Abstract: Cryo electron microscopy facilities running multiple instruments and serving users with varying skill levels need a robust and reliable method for benchmarking both the hardware and software ...Cryo electron microscopy facilities running multiple instruments and serving users with varying skill levels need a robust and reliable method for benchmarking both the hardware and software components of their single particle analysis workflow. The workflow is complex, with many bottlenecks existing at the specimen preparation, data collection and image analysis steps; the samples and grid preparation can be of unpredictable quality, there are many different protocols for microscope and camera settings, and there is a myriad of software programs for analysis that can depend on dozens of settings chosen by the user. For this reason, we believe it is important to benchmark the entire workflow, using a standard sample and standard operating procedures, on a regular basis. This provides confidence that all aspects of the pipeline are capable of producing maps to high resolution. Here we describe benchmarking procedures using a test sample, rabbit muscle aldolase. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_7528.map.gz | 59.5 MB | EMDB map data format | |
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Header (meta data) | emd-7528-v30.xml emd-7528.xml | 12.7 KB 12.7 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_7528_fsc.xml | 10.6 KB | Display | FSC data file |
Images | emd_7528.png | 212.2 KB | ||
Others | emd_7528_half_map_1.map.gz emd_7528_half_map_2.map.gz | 59.1 MB 59.1 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-7528 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-7528 | HTTPS FTP |
-Validation report
Summary document | emd_7528_validation.pdf.gz | 78.4 KB | Display | EMDB validaton report |
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Full document | emd_7528_full_validation.pdf.gz | 77.5 KB | Display | |
Data in XML | emd_7528_validation.xml.gz | 494 B | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-7528 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-7528 | HTTPS FTP |
-Related structure data
Related structure data | 7541C 7550C 7551C 7562C 7614C 7615C 7616C 7617C C: citing same article (ref.) |
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Similar structure data | |
EM raw data | EMPIAR-10184 (Title: Benchmarking cryo-EM single particle analysis workflow Data size: 85.6 Data #1: aligned micrographs of rabbit muscle aldolase from 17dec27a [micrographs - multiframe]) |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_7528.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Rabbit muscle aldolase 17dec27a, 1st 382 images. 2.8A with 87K particles in 11.9 hours. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.855 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: Rabbit muscle aldolase, half map #1
File | emd_7528_half_map_1.map | ||||||||||||
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Annotation | Rabbit muscle aldolase, half map #1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Rabbit muscle aldolase, half map #2
File | emd_7528_half_map_2.map | ||||||||||||
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Annotation | Rabbit muscle aldolase, half map #2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Rabbit muscle aldolase
Entire | Name: Rabbit muscle aldolase |
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Components |
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-Supramolecule #1: Rabbit muscle aldolase
Supramolecule | Name: Rabbit muscle aldolase / type: complex / ID: 1 / Parent: 0 Details: 2.8 A resolution with 87K particles (sorting based on first 382 images) |
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Source (natural) | Organism: Oryctolagus cuniculus (rabbit) |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Molecular weight | Experimental: 150 KDa |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 70.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |