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- EMDB-75286: Closed Mtb-EC: Cryo-EM structure of Mtb RNAP elongation complex (... -

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Basic information

Entry
Database: EMDB / ID: EMD-75286
TitleClosed Mtb-EC: Cryo-EM structure of Mtb RNAP elongation complex (substrate loading mimic) with a closed active site (closed TL and RH-FL)
Map data
Sample
  • Complex: Mtb RNAP elongation complex with a substrate loading mimic
    • Protein or peptide: x 4 types
    • DNA: x 2 types
  • RNA: x 1 types
  • Ligand: x 4 types
KeywordsTranscription / RNA polymerase / DNA/RNA / Nucleotide addition cycle
Function / homology
Function and homology information


Antimicrobial action and antimicrobial resistance in Mtb / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / peptidoglycan-based cell wall / DNA-directed RNA polymerase complex / DNA-templated transcription initiation / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / protein dimerization activity ...Antimicrobial action and antimicrobial resistance in Mtb / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / peptidoglycan-based cell wall / DNA-directed RNA polymerase complex / DNA-templated transcription initiation / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / protein dimerization activity / response to antibiotic / DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / plasma membrane / cytoplasm / cytosol
Similarity search - Function
DNA-directed RNA polymerase, omega subunit / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal / Bacterial RNA polymerase, alpha chain C terminal domain / DNA-directed RNA polymerase beta subunit, bacterial-type / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase, subunit beta-prime ...DNA-directed RNA polymerase, omega subunit / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal / Bacterial RNA polymerase, alpha chain C terminal domain / DNA-directed RNA polymerase beta subunit, bacterial-type / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb6 / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb1, domain 3 superfamily / RPB6/omega subunit-like superfamily / RNA polymerase Rpb1, clamp domain superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb2, domain 2 / RNA polymerase, N-terminal / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase I subunit A N-terminus / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, RBP11-like subunit / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerases beta chain signature. / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain / DNA-directed RNA polymerase, subunit 2 / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain superfamily / RNA polymerase Rpb2, domain 6
Similarity search - Domain/homology
DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase subunit alpha
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria) / Escherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsDhingra Y / Darst SA
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35 GM118130 United States
CitationJournal: bioRxiv / Year: 2026
Title: RNA polymerase inhibitors reveal active-site motions essential for the nucleotide-addition cycle.
Authors: Yukti Dhingra / Robert Landick / Elizabeth A Campbell / Seth A Darst /
Abstract: The nucleotide-addition cycle (NAC) of multi-subunit DNA-dependent RNA polymerases (RNAPs) involves coordinated conformational changes in conserved active-site structural elements, including the ...The nucleotide-addition cycle (NAC) of multi-subunit DNA-dependent RNA polymerases (RNAPs) involves coordinated conformational changes in conserved active-site structural elements, including the trigger loop (TL). The TL is open (unfolded) in most RNAP structures but can close (fold) in substrate-bound (post- or pre-translocated) states of the RNAP, promoting catalysis. TL closure has been associated with closure of another conserved structural element, the Rim-Helices/F-loop (RH-FL), but the role of the RH-FL in the NAC is unclear. Antibiotic leads CBR9379 and AAP-SO inhibit the and RNAPs, respectively, by binding in a pocket formed by the bridge helix and RH-FL. The precise mechanism of action for these inhibitors is yet to be defined. We present cryo-electron microscopy structures showing that both compounds inhibit the RNAP NAC by preventing RH-FL closure, thereby allosterically destabilizing the closed TL. This work reveals a conserved mechanistic principle of RNAP catalysis across all domains of life and provides new insight for antibiotic design.
History
DepositionJan 27, 2026-
Header (metadata) releaseJun 24, 2026-
Map releaseJun 24, 2026-
UpdateJun 24, 2026-
Current statusJun 24, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_75286.png

Downloads & links

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Map

FileDownload / File: emd_75286.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 384 pix.
= 325.248 Å		0.85 Å/pix.
x 384 pix.
= 325.248 Å		0.85 Å/pix.
x 384 pix.
= 325.248 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.847 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.025
Minimum - Maximum-0.080336966 - 0.22395208
Average (Standard dev.)0.0003992846 (±0.006055315)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 325.248 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: local-resolution filtered map

Fileemd_75286_additional_1.map
Annotationlocal-resolution filtered map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Histogram

Histogram (log scale)

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Additional map: sharpened map

Fileemd_75286_additional_2.map
Annotationsharpened map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_75286_half_map_1.map
Projections & Slices
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Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_75286_half_map_2.map
Projections & Slices
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Sample components

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Entire : Mtb RNAP elongation complex with a substrate loading mimic

EntireName: Mtb RNAP elongation complex with a substrate loading mimic
Components
  • Complex: Mtb RNAP elongation complex with a substrate loading mimic
    • Protein or peptide: DNA-directed RNA polymerase subunit alpha
    • Protein or peptide: DNA-directed RNA polymerase subunit omega
    • DNA: Template DNA
    • Protein or peptide: DNA-directed RNA polymerase subunit beta
    • Protein or peptide: DNA-directed RNA polymerase subunit beta'
    • DNA: Non-template DNA
  • RNA: RNA
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION
  • Ligand: GUANOSINE-5'-TRIPHOSPHATE
  • Ligand: water

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Supramolecule #1: Mtb RNAP elongation complex with a substrate loading mimic

SupramoleculeName: Mtb RNAP elongation complex with a substrate loading mimic
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3, #5-#7
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)

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Macromolecule #1: DNA-directed RNA polymerase subunit alpha

MacromoleculeName: DNA-directed RNA polymerase subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 37.745328 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MLISQRPTLS EDVLTDNRSQ FVIEPLEPGF GYTLGNSLRR TLLSSIPGAA VTSIRIDGVL HEFTTVPGVK EDVTEIILNL KSLVVSSEE DEPVTMYLRK QGPGEVTAGD IVPPAGVTVH NPGMHIATLN DKGKLEVELV VERGRGYVPA VQNRASGAEI G RIPVDSIY ...String:
MLISQRPTLS EDVLTDNRSQ FVIEPLEPGF GYTLGNSLRR TLLSSIPGAA VTSIRIDGVL HEFTTVPGVK EDVTEIILNL KSLVVSSEE DEPVTMYLRK QGPGEVTAGD IVPPAGVTVH NPGMHIATLN DKGKLEVELV VERGRGYVPA VQNRASGAEI G RIPVDSIY SPVLKVTYKV DATRVEQRTD FDKLILDVET KNSISPRDAL ASAGKTLVEL FGLARELNVE AEGIEIGPSP AE ADHIASF ALPIDDLDLT VRSYNCLKRE GVHTVGELVA RTESDLLDIR NFGQKSIDEV KIKLHQLGLS LKDSPPSFDP SEV AGYDVA TGTWSTEGAY DEQDYAETEQ L

UniProtKB: DNA-directed RNA polymerase subunit alpha

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Macromolecule #2: DNA-directed RNA polymerase subunit omega

MacromoleculeName: DNA-directed RNA polymerase subunit omega / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 11.85114 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSISQSDASL AAVPAVDQFD PSSGASGGYD TPLGITNPPI DELLDRVSSK YALVIYAAKR ARQINDYYNQ LGEGILEYVG PLVEPGLQE KPLSIALREI HADLLEHTEG E

UniProtKB: DNA-directed RNA polymerase subunit omega

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Macromolecule #5: DNA-directed RNA polymerase subunit beta

MacromoleculeName: DNA-directed RNA polymerase subunit beta / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 130.018828 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MLEGCILADS RQSKTAASPS PSRPQSSSNN SVPGAPNRVS FAKLREPLEV PGLLDVQTDS FEWLIGSPRW RESAAERGDV NPVGGLEEV LYELSPIEDF SGSMSLSFSD PRFDDVKAPV DECKDKDMTY AAPLFVTAEF INNNTGEIKS QTVFMGDFPM M TEKGTFII ...String:
MLEGCILADS RQSKTAASPS PSRPQSSSNN SVPGAPNRVS FAKLREPLEV PGLLDVQTDS FEWLIGSPRW RESAAERGDV NPVGGLEEV LYELSPIEDF SGSMSLSFSD PRFDDVKAPV DECKDKDMTY AAPLFVTAEF INNNTGEIKS QTVFMGDFPM M TEKGTFII NGTERVVVSQ LVRSPGVYFD ETIDKSTDKT LHSVKVIPSR GAWLEFDVDK RDTVGVRIDR KRRQPVTVLL KA LGWTSEQ IVERFGFSEI MRSTLEKDNT VGTDEALLDI YRKLRPGEPP TKESAQTLLE NLFFKEKRYD LARVGRYKVN KKL GLHVGE PITSSTLTEE DVVATIEYLV RLHEGQTTMT VPGGVEVPVE TDDIDHFGNR RLRTVGELIQ NQIRVGMSRM ERVV RERMT TQDVEAITPQ TLINIRPVVA AIKEFFGTSQ LSQFMDQNNP LSGLTHKRRL SALGPGGLSR ERAGLEVRDV HPSHY GRMC PIETPEGPNI GLIGSLSVYA RVNPFGFIET PYRKVVDGVV SDEIVYLTAD EEDRHVVAQA NSPIDADGRF VEPRVL VRR KAGEVEYVPS SEVDYMDVSP RQMVSVATAM IPFLEHDDAN RALMGANMQR QAVPLVRSEA PLVGTGMELR AAIDAGD VV VAEESGVIEE VSADYITVMH DNGTRRTYRM RKFARSNHGT CANQCPIVDA GDRVEAGQVI ADGPCTDDGE MALGKNLL V AIMPWEGHNY EDAIILSNRL VEEDVLTSIH IEEHEIDARD TKLGAEEITR DIPNISDEVL ADLDERGIVR IGAEVRDGD ILVGKVTPKG ETELTPEERL LRAIFGEKAR EVRDTSLKVP HGESGKVIGI RVFSREDEDE LPAGVNELVR VYVAQKRKIS DGDKLAGRH GNKGVIGKIL PVEDMPFLAD GTPVDIILNT HGVPRRMNIG QILETHLGWC AHSGWKVDAA KGVPDWAARL P DELLEAQP NAIVSTPVFD GAQEAELQGL LSCTLPNRDG DVLVDADGKA MLFDGRSGEP FPYPVTVGYM YIMKLHHLVD DK IHARSTG PYSMITQQPL GGKAQFGGQR FGEMECWAMQ AYGAAYTLQE LLTIKSDDTV GRVKVYEAIV KGENIPEPGI PES FKVLLK ELQSLCLNVE VLSSDGAAIE LREGEDEDLE RAAANLGINL SRNESASVED LA

UniProtKB: DNA-directed RNA polymerase subunit beta

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Macromolecule #6: DNA-directed RNA polymerase subunit beta'

MacromoleculeName: DNA-directed RNA polymerase subunit beta' / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 147.097094 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GAMLDVNFFD ELRIGLATAE DIRQWSYGEV KKPETINYRT LKPEKDGLFC EKIFGPTRDW ECYCGKYKRV RFKGIICERC GVEVTRAKV RRERMGHIEL AAPVTHIWYF KGVPSRLGYL LDLAPKDLEK IIYFAAYVIT SVDEEMRHNE LSTLEAEMAV E RKAVEDQR ...String:
GAMLDVNFFD ELRIGLATAE DIRQWSYGEV KKPETINYRT LKPEKDGLFC EKIFGPTRDW ECYCGKYKRV RFKGIICERC GVEVTRAKV RRERMGHIEL AAPVTHIWYF KGVPSRLGYL LDLAPKDLEK IIYFAAYVIT SVDEEMRHNE LSTLEAEMAV E RKAVEDQR DGELEARAQK LEADLAELEA EGAKADARRK VRDGGEREMR QIRDRAQREL DRLEDIWSTF TKLAPKQLIV DE NLYRELV DRYGEYFTGA MGAESIQKLI ENFDIDAEAE SLRDVIRNGK GQKKLRALKR LKVVAAFQQS GNSPMGMVLD AVP VIPPEL RPMVQLDGGR FATSDLNDLY RRVINRNNRL KRLIDLGAPE IIVNNEKRML QESVDALFDN GRRGRPVTGP GNRP LKSLS DLLKGKQGRF RQNLLGKRVD YSGRSVIVVG PQLKLHQCGL PKLMALELFK PFVMKRLVDL NHAQNIKSAK RMVER QRPQ VWDVLEEVIA EHPVLLNRAP TLHRLGIQAF EPMLVEGKAI QLHPLVCEAF NADFDGDQMA VHLPLSAEAQ AEARIL MLS SNNILSPASG RPLAMPRLDM VTGLYYLTTE VPGDTGEYQP ASGDHPETGV YSSPAEAIMA ADRGVLSVRA KIKVRLT QL RPPVEIEAEL FGHSGWQPGD AWMAETTLGR VMFNELLPLG YPFVNKQMHK KVQAAIINDL AERYPMIVVA QTVDKLKD A GFYWATRSGV TVSMADVLVP PRKKEILDHY EERADKVEKQ FQRGALNHDE RNEALVEIWK EATDEVGQAL REHYPDDNP IITIVDSGAT GNFTQTRTLA GMKGLVTNPK GEFIPRPVKS SFREGLTVLE YFINTHGARK GLADTALRTA DSGYLTRRLV DVSQDVIVR EHDCQTERGI VVELAERAPD GTLIRDPYIE TSAYARTLGT DAVDEAGNVI VERGQDLGDP EIDALLAAGI T QVKVRSVL TCATSTGVCA TCYGRSMATG KLVDIGEAVG IVAAQSIGEP GTQLTMRTFH QGGVGEDITG GLPRVQELFE AR VPRGKAP IADVTGRVRL EDGERFYKIT IVPDDGGEEV VYDKISKRQR LRVFKHEDGS ERVLSDGDHV EVGQQLMEGS ADP HEVLRV QGPREVQIHL VREVQEVYRA QGVSIHDKHI EVIVRQMLRR VTIIDSGSTE FLPGSLIDRA EFEAENRRVV AEGG EPAAG RPVLMGITKA SLATDSWLSA ASFQETTRVL TDAAINCRSD KLNGLKENVI IGKLIPAGTG INRYRNIAVQ PTEEA RAAA YTIPSYEDQY YSPDFGAATG AAVPLDDYGY SDYR

UniProtKB: DNA-directed RNA polymerase subunit beta'

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Macromolecule #3: Template DNA

MacromoleculeName: Template DNA / type: dna / ID: 3 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 16.506547 KDa
SequenceString: (DC)(DC)(DG)(DG)(DC)(DA)(DT)(DG)(DA)(DG) (DA)(DG)(DG)(DG)(DT)(DA)(DT)(DT)(DC)(DG) (DC)(DC)(DG)(DC)(DC)(DC)(DA)(DC)(DC) (DT)(DC)(DT)(DC)(DC)(DT)(DA)(DG)(DC)(DC) (DC) (DG)(DC)(DA)(DA)(DG)(DT) ...String:
(DC)(DC)(DG)(DG)(DC)(DA)(DT)(DG)(DA)(DG) (DA)(DG)(DG)(DG)(DT)(DA)(DT)(DT)(DC)(DG) (DC)(DC)(DG)(DC)(DC)(DC)(DA)(DC)(DC) (DT)(DC)(DT)(DC)(DC)(DT)(DA)(DG)(DC)(DC) (DC) (DG)(DC)(DA)(DA)(DG)(DT)(DA)(DT) (DC)(DC)(DG)(DA)(DC)(DG)

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Macromolecule #7: Non-template DNA

MacromoleculeName: Non-template DNA / type: dna / ID: 7 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 16.589572 KDa
SequenceString: (DC)(DG)(DT)(DC)(DG)(DG)(DA)(DT)(DA)(DC) (DT)(DT)(DG)(DC)(DG)(DG)(DG)(DC)(DT)(DA) (DG)(DC)(DC)(DT)(DC)(DT)(DT)(DT)(DT) (DG)(DG)(DC)(DG)(DG)(DC)(DG)(DA)(DA)(DT) (DA) (DC)(DC)(DC)(DT)(DC)(DT) ...String:
(DC)(DG)(DT)(DC)(DG)(DG)(DA)(DT)(DA)(DC) (DT)(DT)(DG)(DC)(DG)(DG)(DG)(DC)(DT)(DA) (DG)(DC)(DC)(DT)(DC)(DT)(DT)(DT)(DT) (DG)(DG)(DC)(DG)(DG)(DC)(DG)(DA)(DA)(DT) (DA) (DC)(DC)(DC)(DT)(DC)(DT)(DC)(DA) (DT)(DG)(DC)(DC)(DG)(DG)

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Macromolecule #4: RNA

MacromoleculeName: RNA / type: rna / ID: 4 / Number of copies: 1
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 6.525968 KDa
SequenceString:
GCAUUCAAAG CGGAGAGGUG

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Macromolecule #8: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 8 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #9: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 9 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #10: GUANOSINE-5'-TRIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 10 / Number of copies: 1 / Formula: GTP
Molecular weightTheoretical: 523.18 Da
Chemical component information

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

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Macromolecule #11: water

MacromoleculeName: water / type: ligand / ID: 11 / Number of copies: 904 / 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: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.7 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 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: PDB ENTRY
PDB model - PDB ID:

8e95

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 274167
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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