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- PDB-9y3p: Eukaryotic translation initiation factor 2-B in its apo form (act... -

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Basic information

Entry
Database: PDB / ID: 9y3p
TitleEukaryotic translation initiation factor 2-B in its apo form (active-state)
Components
  • (Translation initiation factor eIF2B subunit ...) x 5
  • Translation initiation factor eIF-2B subunit alpha
KeywordsTRANSLATION / Guanine nucleotide exchange factor / GEF / initiation
Function / homology
Function and homology information


eukaryotic translation initiation factor 2B complex / Recycling of eIF2:GDP / astrocyte development / astrocyte differentiation / oligodendrocyte development / regulation of translational initiation / cytoplasmic translational initiation / ovarian follicle development / response to glucose / positive regulation of translational initiation ...eukaryotic translation initiation factor 2B complex / Recycling of eIF2:GDP / astrocyte development / astrocyte differentiation / oligodendrocyte development / regulation of translational initiation / cytoplasmic translational initiation / ovarian follicle development / response to glucose / positive regulation of translational initiation / myelination / translation initiation factor activity / translation initiation factor binding / guanyl-nucleotide exchange factor activity / response to endoplasmic reticulum stress / hippocampus development / central nervous system development / translational initiation / response to peptide hormone / T cell receptor signaling pathway / regulation of translation / response to heat / positive regulation of apoptotic process / GTP binding / ATP binding / membrane / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Translation initiation factor eIF-2B subunit alpha, N-terminal / Translation initiation factor eIF-2B subunit epsilon, N-terminal / Translation initiation factor eIF-2B subunit epsilon, W2 domain / : / : / : / : / : / EIF2B subunit epsilon LbH domain / Initiation factor 2B-related ...Translation initiation factor eIF-2B subunit alpha, N-terminal / Translation initiation factor eIF-2B subunit epsilon, N-terminal / Translation initiation factor eIF-2B subunit epsilon, W2 domain / : / : / : / : / : / EIF2B subunit epsilon LbH domain / Initiation factor 2B-related / Initiation factor 2B-like, C-terminal / Initiation factor 2 subunit family / eIF4-gamma/eIF5/eIF2-epsilon / Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5 / W2 domain / W2 domain profile. / Nucleotidyl transferase domain / Nucleotidyl transferase / NagB/RpiA transferase-like / Trimeric LpxA-like superfamily / Nucleotide-diphospho-sugar transferases / Armadillo-type fold
Similarity search - Domain/homology
IMIDAZOLE / Translation initiation factor eIF2B subunit beta / Translation initiation factor eIF2B subunit epsilon / Translation initiation factor eIF2B subunit alpha / Translation initiation factor eIF2B subunit gamma / Translation initiation factor eIF2B subunit delta
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsDalwadi, U. / Croll, T. / Subramanian, A. / Lee, D.J. / Arthur, C. / Walter, P. / Frost, A.
Funding support United States, 1items
OrganizationGrant numberCountry
Other private United States
CitationJournal: Nat Chem Biol / Year: 2026
Title: Allosteric disordering of eIF2B regulates the integrated stress response.
Authors: Udit Dalwadi / Advait Subramanian / Aniliese Deal / Julia E Conrad / Tamara Nadjsombati / Meera Venkatesh / Morgane Boone / Pascal F Egea / Lingjie He / Nimit Jain / D John Lee / Yuwei Liu / ...Authors: Udit Dalwadi / Advait Subramanian / Aniliese Deal / Julia E Conrad / Tamara Nadjsombati / Meera Venkatesh / Morgane Boone / Pascal F Egea / Lingjie He / Nimit Jain / D John Lee / Yuwei Liu / Lucas C Reineke / Kazuki Saito / Nathaniel Talledge / Hannah Toutkoushian / Maxence Le Vasseur / Francesca Zappa / Raoul J de Groot / Diego Acosta-Alvear / Christopher P Arthur / Jodi Nunnari / Susan Marqusee / Rosalie E Lawrence / Mauro Costa-Mattioli / James J Crawford / Frank J M van Kuppeveld / Tristan I Croll / Peter Walter / Adam Frost /
Abstract: The ternary complex, composed of eIF2, GTP and initiator methionyl-tRNA, delivers the first amino acid to the ribosome to initiate protein synthesis. Eukaryotic initiation factor 2B (eIF2B) catalyzes ...The ternary complex, composed of eIF2, GTP and initiator methionyl-tRNA, delivers the first amino acid to the ribosome to initiate protein synthesis. Eukaryotic initiation factor 2B (eIF2B) catalyzes GDP to GTP exchange on eIF2, thereby setting the ternary complex level. Stress-induced phosphorylation converts eIF2 from the substrate of eIF2B into an inhibitor (eIF2-P). This conversion reduces ternary complex levels and induces the integrated stress response (ISR). Here we chart an allosteric axis running through eIF2B, revealing the importance of an α-helix in its β-subunit, the 'latch-helix', that hooks onto the α-subunit to induce eIF2B activity. eIF2-P binding promotes latch-helix unhooking, opening eIF2B, which inhibits its activity. Convergently evolved viral proteins stabilize this latch-helix-binding active state of eIF2B. Using these insights, we generated ISR-activating compounds that stabilize eIF2B in its inhibited, unlatched state. Our study thus highlights how long-range eIF2B allostery can be pharmacologically manipulated to sustain or attenuate the ISR.
History
DepositionSep 2, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 24, 2026Provider: repository / Type: Initial release
Revision 1.0Jun 24, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jun 24, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Jun 24, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
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Revision 1.0Jun 24, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
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Revision 1.2Jul 15, 2026Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Database references / Experimental summary / Data content type: EM metadata / EM metadata / Category: citation / em_admin / Data content type: EM metadata / EM metadata / EM metadata
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Translation initiation factor eIF2B subunit epsilon
B: Translation initiation factor eIF2B subunit epsilon
C: Translation initiation factor eIF2B subunit beta
D: Translation initiation factor eIF2B subunit beta
E: Translation initiation factor eIF2B subunit delta
F: Translation initiation factor eIF2B subunit delta
G: Translation initiation factor eIF-2B subunit alpha
H: Translation initiation factor eIF-2B subunit alpha
I: Translation initiation factor eIF2B subunit gamma
J: Translation initiation factor eIF2B subunit gamma
hetero molecules


Theoretical massNumber of molelcules
Total (without water)425,44425
Polymers424,78510
Non-polymers65915
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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Translation initiation factor eIF2B subunit ... , 5 types, 8 molecules ABCDEFIJ

#1: Protein Translation initiation factor eIF2B subunit epsilon / eIF2B GDP-GTP exchange factor subunit epsilon


Mass: 51385.105 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EIF2B5, EIF2BE / Production host: Escherichia coli (E. coli) / References: UniProt: Q13144
#2: Protein Translation initiation factor eIF2B subunit beta / S20I15 / S20III15 / eIF2B GDP-GTP exchange factor subunit beta


Mass: 38395.773 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EIF2B2, EIF2BB / Production host: Escherichia coli (E. coli) / References: UniProt: P49770
#3: Protein Translation initiation factor eIF2B subunit delta / eIF2B GDP-GTP exchange factor subunit delta


Mass: 39617.582 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EIF2B4, EIF2BD / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UI10
#4: Protein Translation initiation factor eIF2B subunit delta / eIF2B GDP-GTP exchange factor subunit delta


Mass: 39489.453 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EIF2B4, EIF2BD / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UI10
#6: Protein Translation initiation factor eIF2B subunit gamma / eIF2B GDP-GTP exchange factor subunit gamma


Mass: 49304.109 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EIF2B3 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9NR50

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Protein , 1 types, 2 molecules GH

#5: Protein Translation initiation factor eIF-2B subunit alpha / eIF-2B GDP-GTP exchange factor subunit alpha


Mass: 33754.148 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EIF2B1, EIF2BA / Production host: Escherichia coli (E. coli) / References: UniProt: Q14232

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Non-polymers , 3 types, 15 molecules

#7: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: Cl
#8: Chemical ChemComp-IMD / IMIDAZOLE


Mass: 69.085 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H5N2
#9: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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Details

Has ligand of interestN
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Eukaryotic translation initiation factor 2B / Type: COMPLEX / Entity ID: #1-#6 / Source: RECOMBINANT
Molecular weightValue: 0.521758 MDa / Experimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.4
Details: 20 mM HEPES KOH pH 7.4, 200 mM KCl, 5 mM MgCl2, 1 mM TCEP
Buffer component
IDConc.NameFormulaBuffer-ID
120 mM2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid or 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidHEPES1
2200 mMPotassium ChlorideKCl1
35 mMMagnesium ChlorideMgCl21
41 mMtris(2-carboxyethyl)phosphineTCEP1
SpecimenConc.: 6 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 277 K

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Electron microscopy imaging

MicroscopyModel: TFS GLACIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: 1600 nm / Nominal defocus min: 600 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 50 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) / Num. of grids imaged: 2 / Num. of real images: 18826
EM imaging opticsEnergyfilter name: TFS Selectris / Energyfilter slit width: 10 eV
Image scansWidth: 4096 / Height: 4096

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Processing

EM software
IDNameVersionCategory
1cryoSPARC4.2.1particle selection
2EPUimage acquisition
4cryoSPARC4.2.1CTF correction
7ISOLDEmodel fitting
9Servalcatmodel refinement
10cryoSPARC4.2.1initial Euler assignment
11cryoSPARC4.2.1final Euler assignment
12cryoSPARC4.2.1classification
13cryoSPARC4.2.13D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 890578
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 60012 / Symmetry type: POINT
Atomic model buildingProtocol: AB INITIO MODEL
Atomic model buildingPDB-ID: 7L7G

7l7g


Accession code: 7L7G / Source name: PDB / Type: experimental model
RefinementResolution: 2.9→457.523 Å / Num. reflection obs: 8225149 / Average fsc work: 0.789
Displacement parametersBiso mean: 64.4 Å2
Refine LS restraints
Refine-IDTypeDev idealNumberWeight
ELECTRON MICROSCOPYs_bond_nonh_d0.008294590.0119
ELECTRON MICROSCOPYs_angle_nonh_deg1.7153399101.8236
ELECTRON MICROSCOPYs_dihedral_angle_1_deg7.391236935
ELECTRON MICROSCOPYs_dihedral_angle_2_deg3.98498995
ELECTRON MICROSCOPYs_dihedral_angle_3_deg11.1609793210
ELECTRON MICROSCOPYs_dihedral_angle_6_deg15.0625146310
ELECTRON MICROSCOPYs_chiral_restr0.067546570.131
ELECTRON MICROSCOPYs_planes0.0053408960.02
ELECTRON MICROSCOPYs_nbd0.2104412670.2
ELECTRON MICROSCOPYs_nbtor0.2263529060.2
ELECTRON MICROSCOPYs_hbond_nbd0.11587030.2
ELECTRON MICROSCOPYs_metal_ion0.225830.2
LS refinement shell
Resolution (Å)Refine-IDNum. reflection obsFsc work
2.9-2.923ELECTRON MICROSCOPY1969330.4135
2.923-2.942ELECTRON MICROSCOPY1529290.4494
2.942-2.961ELECTRON MICROSCOPY1499790.4766
2.961-2.981ELECTRON MICROSCOPY1497490.4957
2.981-3ELECTRON MICROSCOPY1472370.5092
3-3.02ELECTRON MICROSCOPY1449430.5238
3.02-3.04ELECTRON MICROSCOPY1425850.54
3.04-3.06ELECTRON MICROSCOPY1414170.5592
3.06-3.081ELECTRON MICROSCOPY1400950.576
3.081-3.102ELECTRON MICROSCOPY1377930.5935
3.102-3.123ELECTRON MICROSCOPY1357810.6118
3.123-3.144ELECTRON MICROSCOPY1343610.6285
3.145-3.166ELECTRON MICROSCOPY1324870.6452
3.166-3.188ELECTRON MICROSCOPY1301770.6634
3.188-3.211ELECTRON MICROSCOPY1272090.6809
3.211-3.233ELECTRON MICROSCOPY1273510.6975
3.233-3.256ELECTRON MICROSCOPY1249530.7125
3.256-3.28ELECTRON MICROSCOPY1234090.7275
3.28-3.303ELECTRON MICROSCOPY1207090.741
3.303-3.327ELECTRON MICROSCOPY1191990.7523
3.327-3.352ELECTRON MICROSCOPY1189090.7656
3.352-3.376ELECTRON MICROSCOPY1164810.779
3.377-3.402ELECTRON MICROSCOPY1136470.7921
3.402-3.427ELECTRON MICROSCOPY1131570.8048
3.427-3.453ELECTRON MICROSCOPY1107610.8149
3.453-3.479ELECTRON MICROSCOPY1104970.8244
3.479-3.506ELECTRON MICROSCOPY1069590.834
3.506-3.533ELECTRON MICROSCOPY1062130.8434
3.533-3.56ELECTRON MICROSCOPY1053330.8529
3.561-3.588ELECTRON MICROSCOPY1027510.8596
3.588-3.617ELECTRON MICROSCOPY1010250.8654
3.617-3.645ELECTRON MICROSCOPY990370.8696
3.646-3.675ELECTRON MICROSCOPY991270.8749
3.675-3.705ELECTRON MICROSCOPY962850.8802
3.705-3.735ELECTRON MICROSCOPY951250.8875
3.735-3.766ELECTRON MICROSCOPY936210.8936
3.766-3.797ELECTRON MICROSCOPY922150.8987
3.797-3.829ELECTRON MICROSCOPY909010.902
3.829-3.861ELECTRON MICROSCOPY883890.9049
3.861-3.893ELECTRON MICROSCOPY869470.9062
3.894-3.927ELECTRON MICROSCOPY864930.9082
3.927-3.961ELECTRON MICROSCOPY849250.9139
3.961-3.996ELECTRON MICROSCOPY824970.9205
3.996-4.031ELECTRON MICROSCOPY820510.9257
4.031-4.067ELECTRON MICROSCOPY803290.9274
4.067-4.103ELECTRON MICROSCOPY789330.9272
4.103-4.14ELECTRON MICROSCOPY766990.928
4.141-4.178ELECTRON MICROSCOPY759570.9306
4.178-4.217ELECTRON MICROSCOPY753250.9346
4.217-4.256ELECTRON MICROSCOPY731550.9369
4.256-4.296ELECTRON MICROSCOPY717970.9385
4.296-4.337ELECTRON MICROSCOPY702970.9392
4.337-4.378ELECTRON MICROSCOPY702690.9397
4.378-4.42ELECTRON MICROSCOPY669430.9417
4.421-4.463ELECTRON MICROSCOPY668610.9436
4.464-4.507ELECTRON MICROSCOPY654970.9442
4.508-4.552ELECTRON MICROSCOPY640950.9432
4.553-4.598ELECTRON MICROSCOPY629050.9421
4.598-4.644ELECTRON MICROSCOPY610450.9416
4.645-4.692ELECTRON MICROSCOPY611490.9428
4.693-4.741ELECTRON MICROSCOPY593830.9452
4.741-4.791ELECTRON MICROSCOPY579450.9464
4.791-4.841ELECTRON MICROSCOPY561610.9466
4.842-4.893ELECTRON MICROSCOPY553630.9441
4.893-4.946ELECTRON MICROSCOPY542730.9419
4.946-5ELECTRON MICROSCOPY531730.9404
5-5.055ELECTRON MICROSCOPY518850.9381
5.056-5.112ELECTRON MICROSCOPY512950.935
5.112-5.17ELECTRON MICROSCOPY498450.9307
5.17-5.229ELECTRON MICROSCOPY486370.9265
5.229-5.289ELECTRON MICROSCOPY472390.9227
5.289-5.351ELECTRON MICROSCOPY465690.9199
5.351-5.414ELECTRON MICROSCOPY457690.9174
5.415-5.479ELECTRON MICROSCOPY440670.9145
5.48-5.545ELECTRON MICROSCOPY432730.9107
5.546-5.613ELECTRON MICROSCOPY423330.906
5.614-5.683ELECTRON MICROSCOPY415930.901
5.684-5.755ELECTRON MICROSCOPY400150.8943
5.755-5.828ELECTRON MICROSCOPY391890.8888
5.828-5.903ELECTRON MICROSCOPY378610.8863
5.904-5.98ELECTRON MICROSCOPY374550.8859
5.981-6.06ELECTRON MICROSCOPY363730.8825
6.06-6.14ELECTRON MICROSCOPY350130.8762
6.141-6.224ELECTRON MICROSCOPY348490.8705
6.225-6.31ELECTRON MICROSCOPY333430.8665
6.311-6.398ELECTRON MICROSCOPY328650.8651
6.399-6.489ELECTRON MICROSCOPY312850.8636
6.49-6.582ELECTRON MICROSCOPY306030.8643
6.583-6.679ELECTRON MICROSCOPY303130.8677
6.679-6.778ELECTRON MICROSCOPY287410.8668
6.778-6.879ELECTRON MICROSCOPY284550.8587
6.88-6.984ELECTRON MICROSCOPY271570.8504
6.985-7.093ELECTRON MICROSCOPY270450.8456
7.094-7.204ELECTRON MICROSCOPY257770.8451
7.207-7.32ELECTRON MICROSCOPY244350.8508
7.321-7.438ELECTRON MICROSCOPY242770.8593
7.44-7.562ELECTRON MICROSCOPY233170.8661
7.563-7.689ELECTRON MICROSCOPY228510.8685
7.69-7.819ELECTRON MICROSCOPY217450.8692
7.821-7.956ELECTRON MICROSCOPY210330.8682
7.957-8.097ELECTRON MICROSCOPY207130.8669
8.098-8.243ELECTRON MICROSCOPY196470.8655
8.244-8.394ELECTRON MICROSCOPY188410.87
8.395-8.549ELECTRON MICROSCOPY182170.8772
8.552-8.714ELECTRON MICROSCOPY177270.8851
8.715-8.883ELECTRON MICROSCOPY171250.8854
8.886-9.057ELECTRON MICROSCOPY161250.8874
9.06-9.241ELECTRON MICROSCOPY158710.8931
9.243-9.432ELECTRON MICROSCOPY152250.8994
9.434-9.63ELECTRON MICROSCOPY145330.9025
9.633-9.838ELECTRON MICROSCOPY137530.9039
9.84-10.051ELECTRON MICROSCOPY130590.9083
10.056-10.279ELECTRON MICROSCOPY129730.9178
10.285-10.516ELECTRON MICROSCOPY120210.9276
10.518-10.76ELECTRON MICROSCOPY117310.9325
10.766-11.022ELECTRON MICROSCOPY109810.9346
11.025-11.294ELECTRON MICROSCOPY107250.9341
11.298-11.58ELECTRON MICROSCOPY101170.9327
11.584-11.881ELECTRON MICROSCOPY93750.9309
11.885-12.193ELECTRON MICROSCOPY91330.9304
12.202-12.531ELECTRON MICROSCOPY85770.9307
12.536-12.884ELECTRON MICROSCOPY82270.9308
12.889-13.252ELECTRON MICROSCOPY75970.933
13.263-13.653ELECTRON MICROSCOPY73770.9277
13.659-14.073ELECTRON MICROSCOPY69010.9223
14.079-14.519ELECTRON MICROSCOPY63030.9235
14.526-14.995ELECTRON MICROSCOPY60730.9285
15.003-15.494ELECTRON MICROSCOPY56130.9329
15.511-16.046ELECTRON MICROSCOPY52750.9341
16.056-16.629ELECTRON MICROSCOPY49810.9304
16.64-17.244ELECTRON MICROSCOPY45330.9294
17.268-17.932ELECTRON MICROSCOPY43030.9246
17.946-18.663ELECTRON MICROSCOPY40170.9258
18.678-19.456ELECTRON MICROSCOPY35650.9247
19.473-20.319ELECTRON MICROSCOPY33010.9185
20.339-21.24ELECTRON MICROSCOPY29910.9184
21.286-22.298ELECTRON MICROSCOPY28570.9303
22.325-23.44ELECTRON MICROSCOPY25170.9411
23.501-24.668ELECTRON MICROSCOPY21790.9499
24.74-26.112ELECTRON MICROSCOPY20850.954
26.155-27.691ELECTRON MICROSCOPY18610.9573
27.741-29.472ELECTRON MICROSCOPY16690.9594
29.657-31.497ELECTRON MICROSCOPY13110.9614
31.572-33.729ELECTRON MICROSCOPY12490.9674
33.914-36.514ELECTRON MICROSCOPY10890.9808
36.749-39.672ELECTRON MICROSCOPY9070.9865
39.822-43.04ELECTRON MICROSCOPY7290.9876
43.623-47.961ELECTRON MICROSCOPY6250.9886
48.227-53.549ELECTRON MICROSCOPY5710.9902
53.92-60.6ELECTRON MICROSCOPY3810.9914
61.139-69.772ELECTRON MICROSCOPY3010.991
70.597-80.879ELECTRON MICROSCOPY2250.9939
83.532-99.84ELECTRON MICROSCOPY1750.9967
102.305-126.894ELECTRON MICROSCOPY1050.9977
132.076-161.759ELECTRON MICROSCOPY490.9978
186.783-457.523ELECTRON MICROSCOPY400.8785

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