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- EMDB-44333: Cryo-EM structure of human dynactin complex bound to Chlamydia ef... -

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Basic information

Entry
Database: EMDB / ID: EMD-44333
TitleCryo-EM structure of human dynactin complex bound to Chlamydia effector Dre1
Map data
Sample
  • Complex: Human dynactin complex bound to Chlamydia effector Dre1
    • Protein or peptide: x 9 types
    • Ligand: x 3 types
KeywordsHuman dynactin / Chlamydia effector / host-pathogen interaction / MOTOR PROTEIN
Function / homology
Function and homology information


retrograde axonal transport of mitochondrion / dynactin complex / F-actin capping protein complex / WASH complex / positive regulation of norepinephrine uptake / Regulation of CDH1 Function / Formation of the polybromo-BAF (pBAF) complex / Formation of the non-canonical BAF (ncBAF) complex / Formation of the canonical BAF (cBAF) complex / Formation of the embryonic stem cell BAF (esBAF) complex ...retrograde axonal transport of mitochondrion / dynactin complex / F-actin capping protein complex / WASH complex / positive regulation of norepinephrine uptake / Regulation of CDH1 Function / Formation of the polybromo-BAF (pBAF) complex / Formation of the non-canonical BAF (ncBAF) complex / Formation of the canonical BAF (cBAF) complex / Formation of the embryonic stem cell BAF (esBAF) complex / Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) / sperm head-tail coupling apparatus / bBAF complex / cellular response to cytochalasin B / npBAF complex / nBAF complex / brahma complex / regulation of transepithelial transport / cell junction assembly / morphogenesis of a polarized epithelium / Formation of annular gap junctions / Formation of the dystrophin-glycoprotein complex (DGC) / structural constituent of postsynaptic actin cytoskeleton / barbed-end actin filament capping / GBAF complex / Gap junction degradation / Folding of actin by CCT/TriC / melanosome transport / regulation of G0 to G1 transition / Cell-extracellular matrix interactions / protein localization to adherens junction / actin polymerization or depolymerization / dense body / Tat protein binding / postsynaptic actin cytoskeleton / coronary vasculature development / Prefoldin mediated transfer of substrate to CCT/TriC / RHOD GTPase cycle / RSC-type complex / regulation of double-strand break repair / regulation of nucleotide-excision repair / regulation of cell morphogenesis / protein localization to centrosome / Adherens junctions interactions / dynein complex / RHOF GTPase cycle / COPI-independent Golgi-to-ER retrograde traffic / adherens junction assembly / apical protein localization / Sensory processing of sound by inner hair cells of the cochlea / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / tight junction / microtubule associated complex / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / lamellipodium assembly / cytoplasmic dynein complex / ventricular septum development / aorta development / positive regulation of T cell differentiation / mitotic metaphase chromosome alignment / spectrin binding / apical junction complex / positive regulation of double-strand break repair / maintenance of blood-brain barrier / regulation of norepinephrine uptake / nitric-oxide synthase binding / transporter regulator activity / cortical cytoskeleton / positive regulation of stem cell population maintenance / establishment or maintenance of cell polarity / NuA4 histone acetyltransferase complex / Recycling pathway of L1 / dynein complex binding / Regulation of MITF-M-dependent genes involved in pigmentation / brush border / Advanced glycosylation endproduct receptor signaling / regulation of G1/S transition of mitotic cell cycle / EPH-ephrin mediated repulsion of cells / negative regulation of cell differentiation / kinesin binding / RHO GTPases Activate WASPs and WAVEs / regulation of synaptic vesicle endocytosis / positive regulation of myoblast differentiation / RHO GTPases activate IQGAPs / regulation of protein localization to plasma membrane / positive regulation of double-strand break repair via homologous recombination / COPI-mediated anterograde transport / stress fiber / vesicle-mediated transport / EPHB-mediated forward signaling / axon cytoplasm / cytoskeleton organization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / MHC class II antigen presentation / Recruitment of NuMA to mitotic centrosomes / substantia nigra development
Similarity search - Function
Dynactin subunit 4 / Dynactin p62 family / Dynamitin / : / Dynamitin / Dynactin subunit 6 / Dynactin subunit 5 / F-actin-capping protein subunit beta / F-actin capping protein, beta subunit, conserved site / F-actin-capping protein subunit beta, N-terminal domain ...Dynactin subunit 4 / Dynactin p62 family / Dynamitin / : / Dynamitin / Dynactin subunit 6 / Dynactin subunit 5 / F-actin-capping protein subunit beta / F-actin capping protein, beta subunit, conserved site / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit / F-actin capping protein beta subunit signature. / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 1. / F-actin capping protein alpha subunit signature 2. / F-actin-capping protein subunit alpha / F-actin-capping protein subunit alpha/beta / F-actin-capping protein subunit alpha/beta, domain 2 / F-actin capping protein, alpha subunit, domain 1 / F-actin capping protein alpha subunit / Trimeric LpxA-like superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain
Similarity search - Domain/homology
Dynactin subunit 6 / F-actin-capping protein subunit beta / F-actin-capping protein subunit alpha-1 / Actin, cytoplasmic 1 / Alpha-centractin / Dynactin subunit 2 / Dynactin subunit 5 / Actin-related protein 10 / Dynactin subunit 4
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.47 Å
AuthorsPawar KI / Verba KA
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Cell Rep / Year: 2025
Title: The Chlamydia effector Dre1 binds dynactin to reposition host organelles during infection.
Authors: Jessica Sherry / Komal Ishwar Pawar / Lee Dolat / Erin Smith / I-Chang Chang / Khavong Pha / Robyn Kaake / Danielle L Swaney / Clara Herrera / Eleanor McMahon / Robert J Bastidas / Jeffrey R ...Authors: Jessica Sherry / Komal Ishwar Pawar / Lee Dolat / Erin Smith / I-Chang Chang / Khavong Pha / Robyn Kaake / Danielle L Swaney / Clara Herrera / Eleanor McMahon / Robert J Bastidas / Jeffrey R Johnson / Raphael H Valdivia / Nevan J Krogan / Cherilyn A Elwell / Kliment Verba / Joanne N Engel /
Abstract: The obligate intracellular pathogen Chlamydia trachomatis replicates in a specialized membrane-bound compartment where it repositions host organelles during infection to acquire nutrients and evade ...The obligate intracellular pathogen Chlamydia trachomatis replicates in a specialized membrane-bound compartment where it repositions host organelles during infection to acquire nutrients and evade host surveillance. We describe a bacterial effector, Dre1, that binds specifically to dynactin associated with host microtubule organizing centers without globally impeding dynactin function. Dre1 is required to reposition the centrosome, mitotic spindle, Golgi apparatus, and primary cilia around the inclusion and contributes to pathogen fitness in cell-based and mouse models of infection. We utilized Dre1 to affinity purify the megadalton dynactin protein complex and determined the first cryoelectron microscopy (cryo-EM) structure of human dynactin. Our results suggest that Dre1 binds to the pointed end of dynactin and uncovers the first bacterial effector that modulates dynactin function. Our work highlights how a pathogen employs a single effector to evoke targeted, large-scale changes in host cell organization that facilitate pathogen growth without inhibiting host viability.
History
DepositionMar 28, 2024-
Header (metadata) releaseApr 16, 2025-
Map releaseApr 16, 2025-
UpdateApr 16, 2025-
Current statusApr 16, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_44333.png

Downloads & links

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Map

FileDownload / File: emd_44333.map.gz / Format: CCP4 / Size: 2.4 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 864 pix.
= 721.44 Å		0.84 Å/pix.
x 864 pix.
= 721.44 Å		0.84 Å/pix.
x 864 pix.
= 721.44 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.835 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 4.0
Minimum - Maximum-12.272271 - 26.657999
Average (Standard dev.)-0.0059240037 (±1.2173363)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions864864864
Spacing864864864
CellA=B=C: 721.44 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_44333_half_map_1.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_44333_half_map_2.map
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Sample components

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Entire : Human dynactin complex bound to Chlamydia effector Dre1

EntireName: Human dynactin complex bound to Chlamydia effector Dre1
Components
  • Complex: Human dynactin complex bound to Chlamydia effector Dre1
    • Protein or peptide: Alpha-centractin
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Actin-related protein 10
    • Protein or peptide: Dynactin subunit 4
    • Protein or peptide: Dynactin subunit 5
    • Protein or peptide: Dynactin subunit 6
    • Protein or peptide: F-actin-capping protein subunit alpha-1
    • Protein or peptide: F-actin-capping protein subunit beta
    • Protein or peptide: Dynactin subunit 2
    • Ligand: ADENOSINE-5'-DIPHOSPHATE
    • Ligand: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
    • Ligand: ZINC ION

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Supramolecule #1: Human dynactin complex bound to Chlamydia effector Dre1

SupramoleculeName: Human dynactin complex bound to Chlamydia effector Dre1
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.1 MDa

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Macromolecule #1: Alpha-centractin

MacromoleculeName: Alpha-centractin / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 42.670688 KDa
SequenceString: MESYDVIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHVRVMAG ALEGDIFIGP KAEEHRGLLS IRYPMEHGIV KDWNDMERI WQYVYSKDQL QTFSEEHPVL LTEAPLNPRK NRERAAEVFF ETFNVPALFI SMQAVLSLYA TGRTTGVVLD S GDGVTHAV ...String:
MESYDVIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHVRVMAG ALEGDIFIGP KAEEHRGLLS IRYPMEHGIV KDWNDMERI WQYVYSKDQL QTFSEEHPVL LTEAPLNPRK NRERAAEVFF ETFNVPALFI SMQAVLSLYA TGRTTGVVLD S GDGVTHAV PIYEGFAMPH SIMRIDIAGR DVSRFLRLYL RKEGYDFHSS SEFEIVKAIK ERACYLSINP QKDETLETEK AQ YYLPDGS TIEIGPSRFR APELLFRPDL IGEESEGIHE VLVFAIQKSD MDLRRTLFSN IVLSGGSTLF KGFGDRLLSE VKK LAPKDV KIRISAPQER LYSTWIGGSI LASLDTFKKM WVSKKEYEED GARSIHRKTF

UniProtKB: Alpha-centractin

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Macromolecule #2: Actin, cytoplasmic 1

MacromoleculeName: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.78266 KDa
SequenceString: MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG ...String:
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG YALPHAILRL DLAGRDLTDY LMKILTERGY SFTTTAEREI VRDIKEKLCY VALDFEQEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PEALFQPSFL GMESCGIHET TFNSIMKCDV DIRKDLYANT VLSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ISKQEYDESG PSIVHRKCF

UniProtKB: Actin, cytoplasmic 1

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Macromolecule #3: Actin-related protein 10

MacromoleculeName: Actin-related protein 10 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 46.360863 KDa
SequenceString: MPLYEGLGSG GEKTAVVIDL GEAFTKCGFA GETGPRCIIP SVIKRAGMPK PVRVVQYNIN TEELYSYLKE FIHILYFRHL LVNPRDRRV VIIESVLCPS HFRETLTRVL FKYFEVPSVL LAPSHLMALL TLGINSAMVL DCGYRESLVL PIYEGIPVLN C WGALPLGG ...String:
MPLYEGLGSG GEKTAVVIDL GEAFTKCGFA GETGPRCIIP SVIKRAGMPK PVRVVQYNIN TEELYSYLKE FIHILYFRHL LVNPRDRRV VIIESVLCPS HFRETLTRVL FKYFEVPSVL LAPSHLMALL TLGINSAMVL DCGYRESLVL PIYEGIPVLN C WGALPLGG KALHKELETQ LLEQCTVDTS VAKEQSLPSV MGSVPEGVLE DIKARTCFVS DLKRGLKIQA AKFNIDGNNE RP SPPPNVD YPLDGEKILH ILGSIRDSVV EILFEQDNEE QSVATLILDS LIQCPIDTRK QLAENLVVIG GTSMLPGFLH RLL AEIRYL VEKPKYKKAL GTKTFRIHTP PAKANCVAWL GGAIFGALQD ILGSRSVSKE YYNQTGRIPD WCSLNNPPLE MMFD VGKTQ PPLMKRAFST EK

UniProtKB: Actin-related protein 10

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Macromolecule #4: Dynactin subunit 4

MacromoleculeName: Dynactin subunit 4 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 52.409016 KDa
SequenceString: MASLLQSDRV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS AEAKLKKNRC ANCFDCPGCM HTLSTRATS ISTQLPDDPA KTTMKKAYYL ACGFCRWTSR DVGMADKSVA SGGWQEPENP HTQRMNKLIE YYQQLAQKEK V ERDRKKLA ...String:
MASLLQSDRV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS AEAKLKKNRC ANCFDCPGCM HTLSTRATS ISTQLPDDPA KTTMKKAYYL ACGFCRWTSR DVGMADKSVA SGGWQEPENP HTQRMNKLIE YYQQLAQKEK V ERDRKKLA RRRNYMPLAF SDKYGLGTRL QRPRAGASIS TLAGLSLKEG EDQKEIKIEP AQAVDEVEPL PEDYYTRPVN LT EVTTLQQ RLLQPDFQPV CASQLYPRHK HLLIKRSLRC RKCEHNLSKP EFNPTSIKFK IQLVAVNYIP EVRIMSIPNL RYM KESQVL LTLTNPVENL THVTLFECEE GDPDDINSTA KVVVPPKELV LAGKDAAAEY DELAEPQDFQ DDPDIIAFRK ANKV GIFIK VTPQREEGEV TVCFKMKHDF KNLAAPIRPI EESDQGTEVI WLTQHVELSL GPLLP

UniProtKB: Dynactin subunit 4

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Macromolecule #5: Dynactin subunit 5

MacromoleculeName: Dynactin subunit 5 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 20.150533 KDa
SequenceString:
MELGELLYNK SEYIETASGN KVSRQSVLCG SQNIVLNGKT IVMNDCIIRG DLANVRVGRH CVVKSRSVIR PPFKKFSKGV AFFPLHIGD HVFIEEDCVV NAAQIGSYVH VGKNCVIGRR CVLKDCCKIL DNTVLPPETV VPPFTVFSGC PGLFSGELPE C TQELMIDV TKSYYQKFLP LTQV

UniProtKB: Dynactin subunit 5

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Macromolecule #6: Dynactin subunit 6

MacromoleculeName: Dynactin subunit 6 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 20.769002 KDa
SequenceString:
MAEKTQKSVK IAPGAVVCVE SEIRGDVTIG PRTVIHPKAR IIAEAGPIVI GEGNLIEEQA LIINAYPDNI TPDTEDPEPK PMIIGTNNV FEVGCYSQAM KMGDNNVIES KAYVGRNVIL TSGCIIGACC NLNTFEVIPE NTVIYGADCL RRVQTERPQP Q TLQLDFLM KILPNYHHLK KTMKGSSTPV KN

UniProtKB: Dynactin subunit 6

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Macromolecule #7: F-actin-capping protein subunit alpha-1

MacromoleculeName: F-actin-capping protein subunit alpha-1 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 32.964727 KDa
SequenceString: MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLD PRNKISFKFD HLRKEASDPQ PEEADGGLKS WRESCDSALR AYVKDHYSNG FCTVYAKTID GQQTIIACIE S HQFQPKNF ...String:
MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLD PRNKISFKFD HLRKEASDPQ PEEADGGLKS WRESCDSALR AYVKDHYSNG FCTVYAKTID GQQTIIACIE S HQFQPKNF WNGRWRSEWK FTITPPTAQV VGVLKIQVHY YEDGNVQLVS HKDVQDSLTV SNEAQTAKEF IKIIENAENE YQ TAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA

UniProtKB: F-actin-capping protein subunit alpha-1

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Macromolecule #8: F-actin-capping protein subunit beta

MacromoleculeName: F-actin-capping protein subunit beta / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 30.669768 KDa
SequenceString: MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMP SARLRKLEVE ANNAFDQYRD LYFEGGVSSV YLWDLDHGFA GVILIKKAGD GSKKIKGCWD SIHVVEVQEK S SGRTAHYK ...String:
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL LCDYNRDGDS YRSPWSNKYD PPLEDGAMP SARLRKLEVE ANNAFDQYRD LYFEGGVSSV YLWDLDHGFA GVILIKKAGD GSKKIKGCWD SIHVVEVQEK S SGRTAHYK LTSTVMLWLQ TNKSGSGTMN LGGSLTRQME KDETVSDCSP HIANIGRLVE DMENKIRSTL NEIYFGKTKD IV NGLRSVQ TFADKSKQEA LKNDLVEALK RKQQC

UniProtKB: F-actin-capping protein subunit beta

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Macromolecule #9: Dynactin subunit 2

MacromoleculeName: Dynactin subunit 2 / type: protein_or_peptide / ID: 9 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.285891 KDa
SequenceString: MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELTS TSVEHIIVNP NAAYDKFKDK RVGTKGLDFS DRIGKTKRTG YESGEYEML GEGLGVKETP QQKYQRLLHE VQELTTEVEK IKTTVKESAT EEKLTPVLLA KQLAALKQQL VASHLEKLLG P DAAINLTD ...String:
MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELTS TSVEHIIVNP NAAYDKFKDK RVGTKGLDFS DRIGKTKRTG YESGEYEML GEGLGVKETP QQKYQRLLHE VQELTTEVEK IKTTVKESAT EEKLTPVLLA KQLAALKQQL VASHLEKLLG P DAAINLTD PDGALAKRLL LQLEATKNSK GGSGGKTTGT PPDSSLVTYE LHSRPEQDKF SQAAKVAELE KRLTELETAV RC DQDAQNP LSAGLQGACL METVELLQAK VSALDLAVLD QVEARLQSVL GKVNEIAKHK ASVEDADTQS KVHQLYETIQ RWS PIASTL PELVQRLVTI KQLHEQAMQF GQLLTHLDTT QQMIANSLKD NTTLLTQVQT TMRENLATVE GNFASIDERM KKLG K

UniProtKB: Dynactin subunit 2

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Macromolecule #10: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 10 / Number of copies: 8 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #11: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER

MacromoleculeName: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / type: ligand / ID: 11 / Number of copies: 1 / Formula: ANP
Molecular weightTheoretical: 506.196 Da
Chemical component information

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

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Macromolecule #12: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 12 / Number of copies: 3 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 57.7 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.47 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 50376
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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