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- EMDB-22531: The Cryo-EM structure of the Glutamate decarboxylase from Escheri... -

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Basic information

Entry
Database: EMDB / ID: EMD-22531
TitleThe Cryo-EM structure of the Glutamate decarboxylase from Escherichia coli
Map data
SampleGlutamate decarboxylase
Function / homology
Function and homology information


glutamate decarboxylase / glutamate decarboxylase activity / glutamate metabolic process / pyridoxal phosphate binding
Pyridoxal phosphate-dependent decarboxylase / Glutamate decarboxylase / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / Pyridoxal-phosphate binding site
Glutamate decarboxylase
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.59 Å
AuthorsSu C-C
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: Nat Methods / Year: 2021
Title: A 'Build and Retrieve' methodology to simultaneously solve cryo-EM structures of membrane proteins.
Authors: Chih-Chia Su / Meinan Lyu / Christopher E Morgan / Jani Reddy Bolla / Carol V Robinson / Edward W Yu /
Abstract: Single-particle cryo-electron microscopy (cryo-EM) has become a powerful technique in the field of structural biology. However, the inability to reliably produce pure, homogeneous membrane protein ...Single-particle cryo-electron microscopy (cryo-EM) has become a powerful technique in the field of structural biology. However, the inability to reliably produce pure, homogeneous membrane protein samples hampers the progress of their structural determination. Here, we develop a bottom-up iterative method, Build and Retrieve (BaR), that enables the identification and determination of cryo-EM structures of a variety of inner and outer membrane proteins, including membrane protein complexes of different sizes and dimensions, from a heterogeneous, impure protein sample. We also use the BaR methodology to elucidate structural information from Escherichia coli K12 crude membrane and raw lysate. The findings demonstrate that it is possible to solve high-resolution structures of a number of relatively small (<100 kDa) and less abundant (<10%) unidentified membrane proteins within a single, heterogeneous sample. Importantly, these results highlight the potential of cryo-EM for systems structural proteomics.
Validation ReportSummary, Full report, XML, About validation report
History
DepositionSep 2, 2020-
Header (metadata) releaseJan 20, 2021-
Map releaseJan 20, 2021-
UpdateJan 20, 2021-
Current statusJan 20, 2021Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.25
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.25
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-7jzh
  • Surface level: 0.25
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_22531.png

Downloads & links

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Map

FileDownload / File: emd_22531.map.gz / Format: CCP4 / Size: 6.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 87 pix.
= 93.96 Å		1.08 Å/pix.
x 139 pix.
= 150.12 Å		1.08 Å/pix.
x 139 pix.
= 150.12 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

generated in cubic-lattice coordinate

Voxel sizeX=Y=Z: 1.08 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.25 / Movie #1: 0.25
Minimum - Maximum-1.4763006 - 2.1033604
Average (Standard dev.)2.1572594e-12 (±0.1655687)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin100106132
Dimensions13913987
Spacing13913987
CellA: 150.12001 Å / B: 150.12001 Å / C: 93.96001 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.081.081.08
M x/y/z13913987
origin x/y/z0.0000.0000.000
length x/y/z150.120150.12093.960
α/β/γ90.00090.00090.000
start NX/NY/NZ107101134
NX/NY/NZ14113986
MAP C/R/S123
start NC/NR/NS106100132
NC/NR/NS13913987
D min/max/mean-1.4762.1030.000

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Supplemental data

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Sample components

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Entire Glutamate decarboxylase

EntireName: Glutamate decarboxylase / Number of components: 2

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Component #1: protein, Glutamate decarboxylase

ProteinName: Glutamate decarboxylase / Recombinant expression: No
SourceSpecies: Escherichia coli (E. coli)

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Component #2: protein, Glutamate decarboxylase

ProteinName: Glutamate decarboxylase / Number of Copies: 6 / Recombinant expression: No
MassTheoretical: 52.727957 kDa
SourceSpecies: Escherichia coli (E. coli)

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Experimental details

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Sample preparation

SpecimenSpecimen state: Particle / Method: cryo EM
Sample solutionSpecimen conc.: 0.5 mg/mL / pH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 50 e/Å2 / Illumination mode: FLOOD BEAM
LensImaging mode: BRIGHT FIELD
Specimen HolderModel: OTHER
CameraDetector: OTHER

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Image processing

ProcessingMethod: single particle reconstruction / Number of projections: 32005
3D reconstructionSoftware: cryoSPARC / Resolution: 3.59 Å / Resolution method: FSC 0.143 CUT-OFF

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Atomic model buiding

Output model

7jzh

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