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- EMDB-40848: The structure of C-terminal protease CtpA-LbcA complex of Pseudom... -

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Basic information

Entry
Database: EMDB / ID: EMD-40848
TitleThe structure of C-terminal protease CtpA-LbcA complex of Pseudomonas aeruginosa
Map data
Sample
  • Complex: CtpA-LbcA complex of Pseudomonas aeruginosa
    • Protein or peptide: x 12 types
KeywordsCtpA / LbcA / C-terminal protease / Pseudomonas aeruginosa / HYDROLASE
Function / homology
Function and homology information


cell envelope organization / cell wall biogenesis / cell envelope / protein secretion by the type III secretion system / outer membrane-bounded periplasmic space / endopeptidase activity / periplasmic space / serine-type endopeptidase activity / signal transduction / proteolysis / plasma membrane
Similarity search - Function
: / Activating protease CtpB N-terminal domain / C-terminal-processing peptidase S41A / tail specific protease / Tail specific protease / Peptidase family S41 / PDZ domain 6 / PDZ domain / Tetratricopeptide repeat / Tetratricopeptide repeat ...: / Activating protease CtpB N-terminal domain / C-terminal-processing peptidase S41A / tail specific protease / Tail specific protease / Peptidase family S41 / PDZ domain 6 / PDZ domain / Tetratricopeptide repeat / Tetratricopeptide repeat / ClpP/crotonase-like domain superfamily / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Tetratricopeptide-like helical domain superfamily
Similarity search - Domain/homology
TPR repeat-containing protein PA4667 / Probable carboxyl-terminal protease
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria) / Escherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.84 Å
AuthorsHsu H-C / Li H
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI136901 United States
CitationJournal: EMBO J / Year: 2024
Title: P. aeruginosa CtpA protease adopts a novel activation mechanism to initiate the proteolytic process.
Authors: Hao-Chi Hsu / Michelle Wang / Amanda Kovach / Andrew J Darwin / Huilin Li /
Abstract: During bacterial cell growth, hydrolases cleave peptide cross-links between strands of the peptidoglycan sacculus to allow new strand insertion. The Pseudomonas aeruginosa carboxyl-terminal ...During bacterial cell growth, hydrolases cleave peptide cross-links between strands of the peptidoglycan sacculus to allow new strand insertion. The Pseudomonas aeruginosa carboxyl-terminal processing protease (CTP) CtpA regulates some of these hydrolases by degrading them. CtpA assembles as an inactive hexamer composed of a trimer-of-dimers, but its lipoprotein binding partner LbcA activates CtpA by an unknown mechanism. Here, we report the cryo-EM structures of the CtpA-LbcA complex. LbcA has an N-terminal adaptor domain that binds to CtpA, and a C-terminal superhelical tetratricopeptide repeat domain. One LbcA molecule attaches to each of the three vertices of a CtpA hexamer. LbcA triggers relocation of the CtpA PDZ domain, remodeling of the substrate binding pocket, and realignment of the catalytic residues. Surprisingly, only one CtpA molecule in a CtpA dimer is activated upon LbcA binding. Also, a long loop from one CtpA dimer inserts into a neighboring dimer to facilitate the proteolytic activity. This work has revealed an activation mechanism for a bacterial CTP that is strikingly different from other CTPs that have been characterized structurally.
History
DepositionMay 22, 2023-
Header (metadata) releaseMar 6, 2024-
Map releaseMar 6, 2024-
UpdateApr 24, 2024-
Current statusApr 24, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_40848.png

Downloads & links

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Map

FileDownload / File: emd_40848.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.24 Å/pix.
x 320 pix.
= 397.44 Å		1.24 Å/pix.
x 320 pix.
= 397.44 Å		1.24 Å/pix.
x 320 pix.
= 397.44 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.242 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-2.855842 - 4.1964555
Average (Standard dev.)0.0012232533 (±0.05401485)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 397.44 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_40848_msk_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Half map: #1

Fileemd_40848_half_map_1.map
Projections & Slices
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Histogram

Histogram (log scale)

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Half map: #2

Fileemd_40848_half_map_2.map
Projections & Slices
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Sample components

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Entire : CtpA-LbcA complex of Pseudomonas aeruginosa

EntireName: CtpA-LbcA complex of Pseudomonas aeruginosa
Components
  • Complex: CtpA-LbcA complex of Pseudomonas aeruginosa
    • Protein or peptide: CtpAS302A
    • Protein or peptide: CtpAS302A
    • Protein or peptide: LbcA
    • Protein or peptide: polyA
    • Protein or peptide: CtpAS302A
    • Protein or peptide: CtpAS302A
    • Protein or peptide: LbcA
    • Protein or peptide: polyA
    • Protein or peptide: CtpAS302A
    • Protein or peptide: CtpAS302A
    • Protein or peptide: LbcA
    • Protein or peptide: polyA

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Supramolecule #1: CtpA-LbcA complex of Pseudomonas aeruginosa

SupramoleculeName: CtpA-LbcA complex of Pseudomonas aeruginosa / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 420 KDa

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Macromolecule #1: CtpAS302A

MacromoleculeName: CtpAS302A / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY ...String:
GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY AYLRITQFQV NTGEEVVKAL NQLRKDNKGR LKGLVLDLRN NPGGVLQSAV EVADAFLTKG LIVYTKGRIA NSELRFSADP ADPSDKVPLV VLINGGSAAA AEIVAGALQD QKRAILMGTD SFGKGSVQTV LPLNNDRALK LTTALYYTPN GRSIQAQGIV PDIEVGRAKV TQERSSFEGF KEADLQGHLA NGNGGADRPT GKRAAPSERP QDSDYQLSQA LSLLKGLSVT RGN

UniProtKB: Probable carboxyl-terminal protease

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Macromolecule #2: CtpAS302A

MacromoleculeName: CtpAS302A / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY ...String:
GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY AYLRITQFQV NTGEEVVKAL NQLRKDNKGR LKGLVLDLRN NPGGVLQSAV EVADAFLTKG LIVYTKGRIA NSELRFSADP ADPSDKVPLV VLINGGSAAA AEIVAGALQD QKRAILMGTD SFGKGSVQTV LPLNNDRALK LTTALYYTPN GRSIQAQGIV PDIEVGRAKV TQERSSFEGF KEADLQGHLA NGNGGADRPT GKRAAPSERP QDSDYQLSQA LSLLKGLSVT RGN

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Macromolecule #3: LbcA

MacromoleculeName: LbcA / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MEDTAVETKA KPEKY GSFS EDSLYSLLVA ELAGQRNRFD IALSNYVVQA QKTRDPGVSE RAFRIAEYLG ADQEAL DTS LLWARSAPDN LDAQRAAAIQ LARAGRYEES MVYMEKVLNG QGDTHFDFLA LSAAETD PD TRAGLLQSFD HLLKKYPNNG QLLFGKALLL ...String:
MEDTAVETKA KPEKY GSFS EDSLYSLLVA ELAGQRNRFD IALSNYVVQA QKTRDPGVSE RAFRIAEYLG ADQEAL DTS LLWARSAPDN LDAQRAAAIQ LARAGRYEES MVYMEKVLNG QGDTHFDFLA LSAAETD PD TRAGLLQSFD HLLKKYPNNG QLLFGKALLL QQDGRPDEAL TLLEDNSASR HEVAPLLL R SRLLQSMKRS DEALPLLKAG IKEHPDDKRV RLAYARLLVE QNRLDDAKAE FAGLVQQFP DDDDLRFSLA LVCLEAQAWD EARIYLEELV ERDSHVDAAH FNLGRLAEEQ KDTARALDEY AQVGPGNDF LPAQLRQTDV LLKAGRVDEA AQRLDKARSE QPDYAIQLYL IEAEALSNND Q QEKAWQAI QEGLKQYPED LNLLYTRSML AEKRNDLAQM EKDLRFVIAR EPDNAMALNA LG YTLADRT TRYGEARELI LKAHKLNPDD PAILDSMGWI NYRQGKLADA ERYLRQALQR YPD HEVAAH LGEVLWAQGR QGDARAIWRE YLDKQPDSDV LRRTIKRLTG AETP

UniProtKB: TPR repeat-containing protein PA4667

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Macromolecule #4: polyA

MacromoleculeName: polyA / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString:
AAAAAAA

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Macromolecule #5: CtpAS302A

MacromoleculeName: CtpAS302A / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY ...String:
GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY AYLRITQFQV NTGEEVVKAL NQLRKDNKGR LKGLVLDLRN NPGGVLQSAV EVADAFLTKG LIVYTKGRIA NSELRFSADP ADPSDKVPLV VLINGGSAAA AEIVAGALQD QKRAILMGTD SFGKGSVQTV LPLNNDRALK LTTALYYTPN GRSIQAQGIV PDIEVGRAKV TQERSSFEGF KEADLQGHLA NGNGGADRPT GKRAAPSERP QDSDYQLSQA LSLLKGLSVT RGN

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Macromolecule #6: CtpAS302A

MacromoleculeName: CtpAS302A / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY ...String:
GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY AYLRITQFQV NTGEEVVKAL NQLRKDNKGR LKGLVLDLRN NPGGVLQSAV EVADAFLTKG LIVYTKGRIA NSELRFSADP ADPSDKVPLV VLINGGSAAA AEIVAGALQD QKRAILMGTD SFGKGSVQTV LPLNNDRALK LTTALYYTPN GRSIQAQGIV PDIEVGRAKV TQERSSFEGF KEADLQGHLA NGNGGADRPT GKRAAPSERP QDSDYQLSQA LSLLKGLSVT RGN

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Macromolecule #7: LbcA

MacromoleculeName: LbcA / type: protein_or_peptide / ID: 7 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MEDTAVETKA KPEKY GSFS EDSLYSLLVA ELAGQRNRFD IALSNYVVQA QKTRDPGVSE RAFRIAEYLG ADQEAL DTS LLWARSAPDN LDAQRAAAIQ LARAGRYEES MVYMEKVLNG QGDTHFDFLA LSAAETD PD TRAGLLQSFD HLLKKYPNNG QLLFGKALLL ...String:
MEDTAVETKA KPEKY GSFS EDSLYSLLVA ELAGQRNRFD IALSNYVVQA QKTRDPGVSE RAFRIAEYLG ADQEAL DTS LLWARSAPDN LDAQRAAAIQ LARAGRYEES MVYMEKVLNG QGDTHFDFLA LSAAETD PD TRAGLLQSFD HLLKKYPNNG QLLFGKALLL QQDGRPDEAL TLLEDNSASR HEVAPLLL R SRLLQSMKRS DEALPLLKAG IKEHPDDKRV RLAYARLLVE QNRLDDAKAE FAGLVQQFP DDDDLRFSLA LVCLEAQAWD EARIYLEELV ERDSHVDAAH FNLGRLAEEQ KDTARALDEY AQVGPGNDF LPAQLRQTDV LLKAGRVDEA AQRLDKARSE QPDYAIQLYL IEAEALSNND Q QEKAWQAI QEGLKQYPED LNLLYTRSML AEKRNDLAQM EKDLRFVIAR EPDNAMALNA LG YTLADRT TRYGEARELI LKAHKLNPDD PAILDSMGWI NYRQGKLADA ERYLRQALQR YPD HEVAAH LGEVLWAQGR QGDARAIWRE YLDKQPDSDV LRRTIKRLTG AETP

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Macromolecule #8: polyA

MacromoleculeName: polyA / type: protein_or_peptide / ID: 8 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString:
AAAAAAA

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Macromolecule #9: CtpAS302A

MacromoleculeName: CtpAS302A / type: protein_or_peptide / ID: 9 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY ...String:
GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY AYLRITQFQV NTGEEVVKAL NQLRKDNKGR LKGLVLDLRN NPGGVLQSAV EVADAFLTKG LIVYTKGRIA NSELRFSADP ADPSDKVPLV VLINGGSAAA AEIVAGALQD QKRAILMGTD SFGKGSVQTV LPLNNDRALK LTTALYYTPN GRSIQAQGIV PDIEVGRAKV TQERSSFEGF KEADLQGHLA NGNGGADRPT GKRAAPSERP QDSDYQLSQA LSLLKGLSVT RGN

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Macromolecule #10: CtpAS302A

MacromoleculeName: CtpAS302A / type: protein_or_peptide / ID: 10 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY ...String:
GSHMSAPLPL DELRTFAEVL DRVKAAYVEP VDDKTLLENA IKGMLSNLDP HSAYLGPEDF AELQESTSGE FGGLGIEVGS EDGFIKVVSP IDDTPAARAG IQPGDLIVQI DGKPTKGQSM TEAVDSMRGK AGSPITLTIV RDGGRPFDVE LKRAIIKVKS VKSQVLEPGY AYLRITQFQV NTGEEVVKAL NQLRKDNKGR LKGLVLDLRN NPGGVLQSAV EVADAFLTKG LIVYTKGRIA NSELRFSADP ADPSDKVPLV VLINGGSAAA AEIVAGALQD QKRAILMGTD SFGKGSVQTV LPLNNDRALK LTTALYYTPN GRSIQAQGIV PDIEVGRAKV TQERSSFEGF KEADLQGHLA NGNGGADRPT GKRAAPSERP QDSDYQLSQA LSLLKGLSVT RGN

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Macromolecule #11: LbcA

MacromoleculeName: LbcA / type: protein_or_peptide / ID: 11 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MEDTAVETKA KPEKY GSFS EDSLYSLLVA ELAGQRNRFD IALSNYVVQA QKTRDPGVSE RAFRIAEYLG ADQEAL DTS LLWARSAPDN LDAQRAAAIQ LARAGRYEES MVYMEKVLNG QGDTHFDFLA LSAAETD PD TRAGLLQSFD HLLKKYPNNG QLLFGKALLL ...String:
MEDTAVETKA KPEKY GSFS EDSLYSLLVA ELAGQRNRFD IALSNYVVQA QKTRDPGVSE RAFRIAEYLG ADQEAL DTS LLWARSAPDN LDAQRAAAIQ LARAGRYEES MVYMEKVLNG QGDTHFDFLA LSAAETD PD TRAGLLQSFD HLLKKYPNNG QLLFGKALLL QQDGRPDEAL TLLEDNSASR HEVAPLLL R SRLLQSMKRS DEALPLLKAG IKEHPDDKRV RLAYARLLVE QNRLDDAKAE FAGLVQQFP DDDDLRFSLA LVCLEAQAWD EARIYLEELV ERDSHVDAAH FNLGRLAEEQ KDTARALDEY AQVGPGNDF LPAQLRQTDV LLKAGRVDEA AQRLDKARSE QPDYAIQLYL IEAEALSNND Q QEKAWQAI QEGLKQYPED LNLLYTRSML AEKRNDLAQM EKDLRFVIAR EPDNAMALNA LG YTLADRT TRYGEARELI LKAHKLNPDD PAILDSMGWI NYRQGKLADA ERYLRQALQR YPD HEVAAH LGEVLWAQGR QGDARAIWRE YLDKQPDSDV LRRTIKRLTG AETP

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Macromolecule #12: polyA

MacromoleculeName: polyA / type: protein_or_peptide / ID: 12 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString:
AAAAAAA

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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

Concentration0.8 mg/mL
BufferpH: 7.5
Component:
ConcentrationNameFormula
20.0 mMTris
100.0 mMKClKCl
5.0 mMMgCl2MgCl2
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: OTHER
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 279 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 11520 pixel / Digitization - Dimensions - Height: 8184 pixel / Number grids imaged: 1 / Number real images: 26257 / Average exposure time: 1.5 sec. / Average electron dose: 66.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 2090314
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

7rqh

Final reconstructionNumber classes used: 4 / Applied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.84 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 2.8) / Number images used: 971786
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 2.8)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 2.8)
Final 3D classificationNumber classes: 4 / Software - Name: cryoSPARC (ver. 2.8)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

7rqh

source_name: PDB, initial_model_type: experimental model

7rqf

source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL / Protocol: AB INITIO MODEL / Overall B value: 162.4

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