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- EMDB-49279: Scaffold attached to quinine-I aptamer (Tonic) local refinement o... -

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Basic information

Entry
Database: EMDB / ID: EMD-49279
TitleScaffold attached to quinine-I aptamer (Tonic) local refinement of core
Map data
Sample
  • Complex: Scaffold attached to quinine-I aptamer (Tonic) local refinement of core
    • RNA: RNA (91-MER)
  • Ligand: POTASSIUM ION
  • Ligand: water
KeywordsSynthetic / aptamer / engineering / riboswitch / RNA
Biological speciessynthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.71 Å
AuthorsJones CP / Ferre-D'Amare AR
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI) United States
CitationJournal: To Be Published
Title: Symmetric scaffolds enable de novo modelling of RNA by cryoEM
Authors: Jones CP / Ferre-D'Amare AR
History
DepositionFeb 18, 2025-
Header (metadata) releaseMar 4, 2026-
Map releaseMar 4, 2026-
UpdateMar 4, 2026-
Current statusMar 4, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_49279.png

Downloads & links

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Map

FileDownload / File: emd_49279.map.gz / Format: CCP4 / Size: 506 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 510 pix.
= 423.3 Å		0.83 Å/pix.
x 510 pix.
= 423.3 Å		0.83 Å/pix.
x 510 pix.
= 423.3 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.3951084 - 1.0513303
Average (Standard dev.)-0.00018095358 (±0.0075203213)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions510510510
Spacing510510510
CellA=B=C: 423.3 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_49279_msk_1.map
Projections & Slices
AxesZYX

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Additional map: #1

Fileemd_49279_additional_1.map
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Half map: #1

Fileemd_49279_half_map_1.map
Projections & Slices
AxesZYX

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Half map: #2

Fileemd_49279_half_map_2.map
Projections & Slices
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Sample components

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Entire : Scaffold attached to quinine-I aptamer (Tonic) local refinement o...

EntireName: Scaffold attached to quinine-I aptamer (Tonic) local refinement of core
Components
  • Complex: Scaffold attached to quinine-I aptamer (Tonic) local refinement of core
    • RNA: RNA (91-MER)
  • Ligand: POTASSIUM ION
  • Ligand: water

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Supramolecule #1: Scaffold attached to quinine-I aptamer (Tonic) local refinement o...

SupramoleculeName: Scaffold attached to quinine-I aptamer (Tonic) local refinement of core
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: synthetic construct (others)

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Macromolecule #1: RNA (91-MER)

MacromoleculeName: RNA (91-MER) / type: rna / ID: 1 / Number of copies: 2
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 53.433723 KDa
SequenceString:
GGGCCACUGU UUCACUGUUG CGCUACAUCU CCGGACGACU CUAUACCGCG UGGAUAUGGC ACGCAACUUC AAGACGGGCA CCGUAAAUG UCCUCGGGCG UCGUCCGGAG GCCACACGAA AGUGUGGAGU GACCAGUGGC CCCACCCUGA AGGUAAACUU G UAGCGC

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Macromolecule #2: POTASSIUM ION

MacromoleculeName: POTASSIUM ION / type: ligand / ID: 2 / Number of copies: 2 / Formula: K
Molecular weightTheoretical: 39.098 Da

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Macromolecule #3: water

MacromoleculeName: water / type: ligand / ID: 3 / Number of copies: 390 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 45.09 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.71 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 1320184
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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