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- PDB-9y4b: Eukaryotic translation initiation factor 2-B (eIF2B) with a trunc... -

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Basic information

Entry
Database: PDB / ID: 9y4b
TitleEukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (active-like-state) bound to the viral effector AcP10
Components
  • (Translation initiation factor eIF-2B subunit ...) x 4
  • Translation initiation factor eIF2B subunit beta
  • Uridine kinase P10
KeywordsTRANSLATION / Guanine nucleotide exchange factor / GEF / initiation
Function / homology
Function and homology information


uridine/cytidine kinase / uridine kinase activity / eukaryotic translation initiation factor 2B complex / Recycling of eIF2:GDP / astrocyte development / astrocyte differentiation / oligodendrocyte development / regulation of translational initiation / cytoplasmic translational initiation / positive regulation of translational initiation ...uridine/cytidine kinase / uridine kinase activity / eukaryotic translation initiation factor 2B complex / Recycling of eIF2:GDP / astrocyte development / astrocyte differentiation / oligodendrocyte development / regulation of translational initiation / cytoplasmic translational initiation / positive regulation of translational initiation / response to glucose / ovarian follicle development / myelination / translation initiation factor activity / translation initiation factor binding / guanyl-nucleotide exchange factor activity / response to endoplasmic reticulum stress / central nervous system development / hippocampus development / translational initiation / response to peptide hormone / regulation of translation / T cell receptor signaling pathway / response to heat / host cell perinuclear region of cytoplasm / positive regulation of apoptotic process / GTP binding / ATP binding / membrane / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Phosphoribulokinase/uridine kinase / Phosphoribulokinase / Uridine kinase family / 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 / : / : / : / : / : ...Phosphoribulokinase/uridine kinase / Phosphoribulokinase / Uridine kinase family / 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 / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
PHOSPHATE ION / Uridine kinase P10 / 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)
Beluga whale coronavirus SW1
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.1 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: To Be Published
Title: Allosteric Disordering of eIF2B Regulates the Integrated Stress Response
Authors: Dalwadi, U. / Croll, T. / Subramanian, A. / Lee, D.J. / Arthur, C. / Walter, P. / Frost, A.
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
Revision 1.0Jun 24, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jun 24, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jun 24, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Translation initiation factor eIF-2B subunit epsilon
B: Translation initiation factor eIF-2B subunit epsilon
C: Translation initiation factor eIF2B subunit beta
D: Translation initiation factor eIF2B subunit beta
E: Translation initiation factor eIF-2B subunit delta
F: Translation initiation factor eIF-2B subunit delta
G: Translation initiation factor eIF-2B subunit alpha
H: Translation initiation factor eIF-2B subunit alpha
I: Translation initiation factor eIF-2B subunit gamma
J: Translation initiation factor eIF-2B subunit gamma
K: Uridine kinase P10
L: Uridine kinase P10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)571,32723
Polymers570,63912
Non-polymers68811
Water362
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 eIF-2B subunit ... , 4 types, 8 molecules ABEFGHIJ

#1: Protein Translation initiation factor eIF-2B subunit epsilon / eIF-2B GDP-GTP exchange factor subunit epsilon


Mass: 80466.609 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
#3: Protein Translation initiation factor eIF-2B subunit delta / eIF-2B GDP-GTP exchange factor subunit delta


Mass: 57640.168 Da / Num. of mol.: 2
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 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
#5: Protein Translation initiation factor eIF-2B subunit gamma / eIF-2B GDP-GTP exchange factor subunit gamma


Mass: 50304.230 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 , 2 types, 4 molecules CDKL

#2: Protein Translation initiation factor eIF2B subunit beta / S20I15 / S20III15 / eIF2B GDP-GTP exchange factor subunit beta


Mass: 39438.922 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: latch-helix deletion / Source: (gene. exp.) Homo sapiens (human) / Gene: EIF2B2, EIF2BB / Production host: Escherichia coli (E. coli) / References: UniProt: P49770
#6: Protein Uridine kinase P10 / Accessory protein P10 / AcP10


Mass: 23715.584 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Beluga whale coronavirus SW1 / Gene: ORF10 / Production host: Escherichia coli (E. coli) / References: UniProt: B2BW43, uridine/cytidine kinase

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Non-polymers , 4 types, 13 molecules

#7: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#8: Chemical
ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: PO4
#9: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: H2O

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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

Component
IDNameTypeEntity IDParent-IDSource
1Eukaryotic translation initiation factor 2B bound to two copies of AcP10COMPLEX#1-#60MULTIPLE SOURCES
2eIF2B (latch-helix deletion)COMPLEX#1-#51RECOMBINANT
3AcP10COMPLEX#61RECOMBINANT
Molecular weight
IDEntity assembly-IDValue (°)Experimental value
110.569120 MDaNO
21521758 kDa/nmNO
3123681 kDa/nmNO
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
21Homo sapiens (human)9606
32Homo sapiens (human)9606
43Beluga whale coronavirus SW1694015
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-ID
21Escherichia coli (E. coli)562
32Escherichia coli (E. coli)562
43Escherichia coli (E. coli)562
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: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 277 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 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: 1 / Num. of real images: 5000
EM imaging opticsEnergyfilter name: TFS Selectris / Energyfilter slit width: 10 eV
Image scansWidth: 4096 / Height: 4096

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Processing

EM software
IDNameVersionCategory
1cryoSPARC4.6.0particle selection
2EPUimage acquisition
4cryoSPARC4.6.0CTF correction
7ISOLDEmodel fitting
9Servalcatmodel refinement
10cryoSPARC4.6.0initial Euler assignment
11cryoSPARC4.6.0final Euler assignment
12cryoSPARC4.6.0classification
13cryoSPARC4.6.03D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 867729
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 2.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 171498 / Num. of class averages: 1 / Symmetry type: POINT
Atomic model buildingProtocol: AB INITIO MODEL
Atomic model building
IDPDB-ID 3D fitting-IDAccession codeInitial refinement model-IDSource nameType
17L7G

7l7g

17L7G1PDBexperimental model
21AF-Q9HA47-F12AlphaFoldin silico model
RefinementResolution: 2.1→2.1 Å / Num. reflection obs: 14475790 / Average fsc work: 0.6643
Displacement parametersBiso mean: 54.84 Å2
Refine LS restraints
Refine-IDTypeDev idealNumberWeight
ELECTRON MICROSCOPYs_bond_nonh_d0.0081327780.0119
ELECTRON MICROSCOPYs_angle_nonh_deg1.6546444161.8235
ELECTRON MICROSCOPYs_dihedral_angle_1_deg6.688540965
ELECTRON MICROSCOPYs_dihedral_angle_2_deg3.57379885
ELECTRON MICROSCOPYs_dihedral_angle_3_deg10.5216877410
ELECTRON MICROSCOPYs_dihedral_angle_6_deg14.8705164210
ELECTRON MICROSCOPYs_chiral_restr0.07551500.131
ELECTRON MICROSCOPYs_planes0.0061454880.02
ELECTRON MICROSCOPYs_nbd0.2078471870.2
ELECTRON MICROSCOPYs_nbtor0.2249583700.2
ELECTRON MICROSCOPYs_hbond_nbd0.11178870.2
LS refinement shell
Resolution (Å)Refine-IDNum. reflection obsFsc work
1.95-1.96ELECTRON MICROSCOPY2222130.2098
1.96-1.97ELECTRON MICROSCOPY2244550.2232
1.971-1.981ELECTRON MICROSCOPY2223690.2364
1.981-1.992ELECTRON MICROSCOPY2197570.2499
1.992-2.002ELECTRON MICROSCOPY2171910.2664
2.002-2.013ELECTRON MICROSCOPY2155690.2856
2.013-2.024ELECTRON MICROSCOPY2125090.3071
2.024-2.035ELECTRON MICROSCOPY2105910.3222
2.035-2.046ELECTRON MICROSCOPY2076730.3366
2.047-2.058ELECTRON MICROSCOPY2064210.3514
2.058-2.069ELECTRON MICROSCOPY2034610.3666
2.069-2.081ELECTRON MICROSCOPY2011110.3802
2.081-2.093ELECTRON MICROSCOPY1997290.3933
2.093-2.104ELECTRON MICROSCOPY1968490.4034
2.104-2.116ELECTRON MICROSCOPY1947870.4169
2.116-2.129ELECTRON MICROSCOPY1909090.4338
2.129-2.141ELECTRON MICROSCOPY1910850.4477
2.141-2.153ELECTRON MICROSCOPY1879930.4601
2.153-2.166ELECTRON MICROSCOPY1858110.472
2.166-2.178ELECTRON MICROSCOPY1829050.4873
2.179-2.191ELECTRON MICROSCOPY1830610.5016
2.191-2.204ELECTRON MICROSCOPY1792830.5138
2.204-2.218ELECTRON MICROSCOPY1772290.5292
2.218-2.231ELECTRON MICROSCOPY1757490.543
2.231-2.244ELECTRON MICROSCOPY1718590.5544
2.244-2.258ELECTRON MICROSCOPY1720330.5653
2.258-2.272ELECTRON MICROSCOPY1679850.5811
2.272-2.286ELECTRON MICROSCOPY1676410.5985
2.286-2.3ELECTRON MICROSCOPY1639950.6086
2.3-2.314ELECTRON MICROSCOPY1642810.6155
2.314-2.329ELECTRON MICROSCOPY1611090.6238
2.329-2.343ELECTRON MICROSCOPY1580230.6357
2.343-2.358ELECTRON MICROSCOPY1565410.6514
2.358-2.373ELECTRON MICROSCOPY1553970.6627
2.373-2.389ELECTRON MICROSCOPY1529290.6702
2.389-2.404ELECTRON MICROSCOPY1499790.6743
2.404-2.42ELECTRON MICROSCOPY1497490.6835
2.42-2.436ELECTRON MICROSCOPY1472370.6971
2.436-2.452ELECTRON MICROSCOPY1449430.7124
2.452-2.468ELECTRON MICROSCOPY1425850.7258
2.468-2.484ELECTRON MICROSCOPY1414170.7348
2.485-2.501ELECTRON MICROSCOPY1400950.7418
2.501-2.518ELECTRON MICROSCOPY1377930.7477
2.518-2.535ELECTRON MICROSCOPY1357810.7518
2.535-2.553ELECTRON MICROSCOPY1343610.7573
2.553-2.57ELECTRON MICROSCOPY1324870.764
2.571-2.588ELECTRON MICROSCOPY1301770.7731
2.589-2.607ELECTRON MICROSCOPY1272090.7826
2.607-2.625ELECTRON MICROSCOPY1273510.7897
2.625-2.644ELECTRON MICROSCOPY1249530.7976
2.644-2.663ELECTRON MICROSCOPY1234090.8046
2.663-2.682ELECTRON MICROSCOPY1207090.8081
2.682-2.701ELECTRON MICROSCOPY1191990.8156
2.701-2.721ELECTRON MICROSCOPY1189090.8246
2.721-2.741ELECTRON MICROSCOPY1164810.8331
2.741-2.762ELECTRON MICROSCOPY1136470.8394
2.762-2.782ELECTRON MICROSCOPY1131570.8452
2.782-2.803ELECTRON MICROSCOPY1107610.8538
2.803-2.825ELECTRON MICROSCOPY1104970.8596
2.825-2.846ELECTRON MICROSCOPY1069590.8615
2.846-2.868ELECTRON MICROSCOPY1062130.8643
2.868-2.891ELECTRON MICROSCOPY1053330.8694
2.891-2.913ELECTRON MICROSCOPY1027510.8735
2.913-2.936ELECTRON MICROSCOPY1010250.8757
2.936-2.96ELECTRON MICROSCOPY990370.8789
2.96-2.983ELECTRON MICROSCOPY991270.885
2.983-3.008ELECTRON MICROSCOPY962850.8905
3.008-3.032ELECTRON MICROSCOPY951250.8936
3.032-3.057ELECTRON MICROSCOPY936210.8958
3.057-3.082ELECTRON MICROSCOPY922150.8989
3.083-3.108ELECTRON MICROSCOPY909010.9029
3.108-3.134ELECTRON MICROSCOPY883890.9072
3.135-3.161ELECTRON MICROSCOPY869470.911
3.161-3.188ELECTRON MICROSCOPY864930.9136
3.188-3.216ELECTRON MICROSCOPY849250.9146
3.216-3.244ELECTRON MICROSCOPY824970.9153
3.244-3.273ELECTRON MICROSCOPY820510.9174
3.273-3.302ELECTRON MICROSCOPY803290.9197
3.302-3.331ELECTRON MICROSCOPY789330.9219
3.331-3.361ELECTRON MICROSCOPY766990.9247
3.361-3.392ELECTRON MICROSCOPY759570.9282
3.392-3.423ELECTRON MICROSCOPY753250.9298
3.424-3.455ELECTRON MICROSCOPY731550.9294
3.455-3.487ELECTRON MICROSCOPY717970.9288
3.488-3.521ELECTRON MICROSCOPY702970.9301
3.521-3.554ELECTRON MICROSCOPY702690.9318
3.554-3.589ELECTRON MICROSCOPY669430.932
3.589-3.624ELECTRON MICROSCOPY668610.9305
3.624-3.659ELECTRON MICROSCOPY654970.93
3.66-3.696ELECTRON MICROSCOPY640950.9324
3.696-3.733ELECTRON MICROSCOPY629050.9363
3.733-3.771ELECTRON MICROSCOPY610450.9389
3.771-3.809ELECTRON MICROSCOPY611490.9388
3.81-3.849ELECTRON MICROSCOPY593830.9362
3.849-3.889ELECTRON MICROSCOPY579450.934
3.889-3.93ELECTRON MICROSCOPY561610.9352
3.931-3.972ELECTRON MICROSCOPY553630.9373
3.973-4.015ELECTRON MICROSCOPY542730.9382
4.016-4.059ELECTRON MICROSCOPY531730.9356
4.06-4.104ELECTRON MICROSCOPY518850.9341
4.104-4.15ELECTRON MICROSCOPY512950.936
4.15-4.197ELECTRON MICROSCOPY498450.9378
4.197-4.245ELECTRON MICROSCOPY486370.9389
4.245-4.294ELECTRON MICROSCOPY472390.9391
4.294-4.344ELECTRON MICROSCOPY465690.9373
4.344-4.396ELECTRON MICROSCOPY457690.9366
4.396-4.448ELECTRON MICROSCOPY440670.9375
4.449-4.502ELECTRON MICROSCOPY432730.9375
4.502-4.557ELECTRON MICROSCOPY423330.9356
4.558-4.614ELECTRON MICROSCOPY415930.9345
4.614-4.672ELECTRON MICROSCOPY400150.9358
4.672-4.731ELECTRON MICROSCOPY391890.9385
4.732-4.792ELECTRON MICROSCOPY378610.9383
4.793-4.855ELECTRON MICROSCOPY374550.9326
4.856-4.919ELECTRON MICROSCOPY363730.9272
4.92-4.985ELECTRON MICROSCOPY350130.926
4.986-5.053ELECTRON MICROSCOPY348490.925
5.054-5.123ELECTRON MICROSCOPY333430.9202
5.123-5.195ELECTRON MICROSCOPY328650.9134
5.195-5.268ELECTRON MICROSCOPY312850.906
5.269-5.343ELECTRON MICROSCOPY306030.9027
5.345-5.422ELECTRON MICROSCOPY303130.9011
5.423-5.502ELECTRON MICROSCOPY287410.8978
5.503-5.584ELECTRON MICROSCOPY284550.8933
5.586-5.67ELECTRON MICROSCOPY271570.8851
5.671-5.758ELECTRON MICROSCOPY270450.8746
5.759-5.849ELECTRON MICROSCOPY257770.866
5.851-5.942ELECTRON MICROSCOPY244350.8618
5.943-6.038ELECTRON MICROSCOPY242770.8596
6.04-6.139ELECTRON MICROSCOPY233170.8531
6.14-6.242ELECTRON MICROSCOPY228510.849
6.243-6.348ELECTRON MICROSCOPY217450.8458
6.35-6.459ELECTRON MICROSCOPY210330.8465
6.46-6.573ELECTRON MICROSCOPY207130.8503
6.574-6.692ELECTRON MICROSCOPY196470.8466
6.693-6.815ELECTRON MICROSCOPY188410.8332
6.816-6.941ELECTRON MICROSCOPY182170.8197
6.943-7.074ELECTRON MICROSCOPY177270.8221
7.075-7.211ELECTRON MICROSCOPY171250.8334
7.214-7.353ELECTRON MICROSCOPY161250.843
7.356-7.503ELECTRON MICROSCOPY158710.849
7.504-7.657ELECTRON MICROSCOPY152250.8518
7.659-7.818ELECTRON MICROSCOPY145330.8512
7.82-7.987ELECTRON MICROSCOPY137530.8435
7.988-8.16ELECTRON MICROSCOPY130590.8355
8.164-8.345ELECTRON MICROSCOPY129730.8357
8.35-8.537ELECTRON MICROSCOPY120210.8446
8.539-8.736ELECTRON MICROSCOPY117310.8543
8.74-8.948ELECTRON MICROSCOPY109810.8614
8.951-9.169ELECTRON MICROSCOPY107250.8696
9.172-9.401ELECTRON MICROSCOPY101170.8802
9.404-9.645ELECTRON MICROSCOPY93750.8861
9.649-9.899ELECTRON MICROSCOPY91330.89
9.906-10.174ELECTRON MICROSCOPY85770.8993
10.177-10.46ELECTRON MICROSCOPY82270.9123
10.464-10.758ELECTRON MICROSCOPY75970.9189
10.768-11.084ELECTRON MICROSCOPY73770.9194
11.089-11.425ELECTRON MICROSCOPY69010.9191
11.43-11.787ELECTRON MICROSCOPY63030.9177
11.793-12.173ELECTRON MICROSCOPY60730.9117
12.18-12.579ELECTRON MICROSCOPY56130.9142
12.593-13.027ELECTRON MICROSCOPY52750.9171
13.035-13.5ELECTRON MICROSCOPY49810.9123
13.509-13.999ELECTRON MICROSCOPY45330.9018
14.019-14.558ELECTRON MICROSCOPY43030.9031
14.569-15.151ELECTRON MICROSCOPY40170.9087
15.164-15.795ELECTRON MICROSCOPY35650.9208
15.81-16.496ELECTRON MICROSCOPY33010.9236
16.513-17.244ELECTRON MICROSCOPY29910.9199
17.281-18.103ELECTRON MICROSCOPY28570.9172
18.124-19.029ELECTRON MICROSCOPY25170.9181
19.08-20.027ELECTRON MICROSCOPY21790.9115
20.085-21.199ELECTRON MICROSCOPY20850.9094
21.234-22.481ELECTRON MICROSCOPY18610.9209
22.522-23.927ELECTRON MICROSCOPY16690.93
24.077-25.571ELECTRON MICROSCOPY13110.9407
25.632-27.383ELECTRON MICROSCOPY12490.9436
27.533-29.644ELECTRON MICROSCOPY10890.9544
29.835-32.208ELECTRON MICROSCOPY9070.9652
32.33-34.942ELECTRON MICROSCOPY7290.9769
35.415-38.937ELECTRON MICROSCOPY6250.9818
39.153-43.474ELECTRON MICROSCOPY5710.9757
43.775-49.198ELECTRON MICROSCOPY3810.9744
49.636-56.644ELECTRON MICROSCOPY3010.9766
57.314-65.662ELECTRON MICROSCOPY2250.9688
67.815-81.055ELECTRON MICROSCOPY1750.9726
83.057-103.019ELECTRON MICROSCOPY1050.9812
107.225-131.324ELECTRON MICROSCOPY490.9864
151.64-371.44ELECTRON MICROSCOPY400.8989

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