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- EMDB-61095: Structure of photosynthetic LH1-RC complex from the purple bacter... -

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Basic information

Entry
Database: EMDB / ID: EMD-61095
TitleStructure of photosynthetic LH1-RC complex from the purple bacterium Blastochloris tepida
Map datafull-map
Sample
  • Complex: Photosynthetic LH1-RC complex of Blastochloris tepida
    • Protein or peptide: x 8 types
  • Ligand: x 14 types
KeywordsLH1-RC COMPLEX / PHOTOSYNTHESIS / PURPLE BACTERIA
Function / homology
Function and homology information


organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / : / endomembrane system / electron transfer activity / iron ion binding ...organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / photosynthesis, light reaction / : / endomembrane system / electron transfer activity / iron ion binding / heme binding / metal ion binding / membrane / plasma membrane
Similarity search - Function
Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Antenna complex, alpha/beta subunit / Light-harvesting protein B beta chain ...Photosynthetic reaction centre, cytochrome c subunit / Multihaem cytochrome, PRC subunit superfamily / Photosynthetic reaction centre cytochrome C subunit / Antenna complex, beta subunit, conserved site / Antenna complexes beta subunits signature. / Antenna complex, alpha subunit / Antenna complex, alpha subunit conserved site / Antenna complexes alpha subunits signature. / Antenna complex, alpha/beta subunit / Light-harvesting protein B beta chain / Antenna complex, beta domain superfamily / Antenna complex alpha/beta subunit / Light-harvesting complex / Photosynthetic reaction centre, H subunit / Bacterial photosynthetic reaction centre, H-chain, C-terminal / Photosynthetic reaction centre, M subunit / Photosynthetic reaction centre, H subunit, N-terminal / Photosynthetic reaction centre, H subunit, N-terminal domain superfamily / Photosynthetic reaction centre, H-chain N-terminal region / PRC-barrel domain / PRC-barrel domain / Photosynthetic reaction centre, L subunit / PRC-barrel-like superfamily / Multiheme cytochrome superfamily / : / Photosynthetic reaction centre, L/M / Photosystem II protein D1/D2 superfamily / Photosynthetic reaction centre protein / Photosynthetic reaction center proteins signature. / Prokaryotic membrane lipoprotein lipid attachment site profile.
Similarity search - Domain/homology
Photosynthetic reaction center subunit H / Antenna complex alpha/beta subunit domain-containing protein / Antenna complex alpha/beta subunit domain-containing protein / Reaction center protein L chain / Reaction center protein M chain / Photosynthetic reaction center cytochrome c subunit / Uncharacterized protein / Light-harvesting protein B-1015 gamma chain
Similarity search - Component
Biological speciesBlastochloris tepida (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.2 Å
AuthorsKimura Y / Kanno R / Mori K / Matsuda Y / Seto R / Takenaka S / Mino H / Ohkubo T / Honda M / Sasaki YC ...Kimura Y / Kanno R / Mori K / Matsuda Y / Seto R / Takenaka S / Mino H / Ohkubo T / Honda M / Sasaki YC / Kishikawa J / Mitsuoka K / Mio K / Hall M / Purba ER / Mochizuki T / Mizoguchi A / Humbel BM / Madigan MT / Wang-Otomo Z-Y / Tani K
Funding support Japan, 6 items
OrganizationGrant numberCountry
Japan Agency for Medical Research and Development (AMED)JP21am0101118 Japan
Japan Agency for Medical Research and Development (AMED)JP21am0101116 Japan
Japan Society for the Promotion of Science (JSPS)JP16H04174 Japan
Japan Society for the Promotion of Science (JSPS)JP18H05153 Japan
Japan Society for the Promotion of Science (JSPS)20H05086 Japan
Japan Society for the Promotion of Science (JSPS)20H02856 Japan
CitationJournal: Biochemistry / Year: 2025
Title: The Thermal-Stable LH1-RC Complex of a Hot Spring Purple Bacterium Powers Photosynthesis with Extremely Low-Energy Near-Infrared Light.
Authors: Yukihiro Kimura / Ryo Kanno / Kaisei Mori / Yoshiki Matsuda / Ryuta Seto / Shinji Takenaka / Hiroyuki Mino / Tatsunari Ohkubo / Mai Honda / Yuji C Sasaki / Jun-Ichi Kishikawa / Kaoru ...Authors: Yukihiro Kimura / Ryo Kanno / Kaisei Mori / Yoshiki Matsuda / Ryuta Seto / Shinji Takenaka / Hiroyuki Mino / Tatsunari Ohkubo / Mai Honda / Yuji C Sasaki / Jun-Ichi Kishikawa / Kaoru Mitsuoka / Kazuhiro Mio / Malgorzata Hall / Endang R Purba / Toshiaki Mochizuki / Akira Mizoguchi / Bruno M Humbel / Michael T Madigan / Zheng-Yu Wang-Otomo / Kazutoshi Tani /
Abstract: is a hot spring purple nonsulfur phototrophic bacterium that contains bacteriochlorophyll (BChl) . Here, we present a 2.21 Å cryo-EM structure of the thermostable light-harvesting 1-reaction center ... is a hot spring purple nonsulfur phototrophic bacterium that contains bacteriochlorophyll (BChl) . Here, we present a 2.21 Å cryo-EM structure of the thermostable light-harvesting 1-reaction center (LH1-RC) complex from . The LH1 ring comprises 16 circularly arranged αβγ-subunits plus one αβ-subunit that surround the RC complex composed of C-, H-, L-, and M-subunits. In a comparative study, the LH1-RC showed numerous electrostatic and hydrophobic interactions both within the LH1 complex itself and between the LH1 and the RC complexes that are absent from the LH1-RC complex of its mesophilic counterpart, . These additional interactions result in a tightly packed LH1-RC architecture with a reduced accessible surface area per volume that enhances the thermal stability of the complex and allows the light reactions of photosynthesis to proceed at hot spring temperatures. Moreover, based on high-resolution structural information combined with spectroscopic evidence, the unique photosynthetic property of the LH1-RC─absorption of energy-poor near-infrared light beyond 1000 nm─can be attributed to strong hydrogen-bonding interactions between the C3-acetyl C═O of the LH1 BChl and two LH1 α-Trp residues, structural rigidity of the LH1, and the enhanced exciton coupling of the LH1 BChls of this thermophile.
History
DepositionAug 6, 2024-
Header (metadata) releaseDec 18, 2024-
Map releaseDec 18, 2024-
UpdateApr 23, 2025-
Current statusApr 23, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_61095.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationfull-map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 400 pix.
= 328. Å
0.82 Å/pix.
x 400 pix.
= 328. Å
0.82 Å/pix.
x 400 pix.
= 328. Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.82 Å
Density
Contour LevelBy AUTHOR: 0.045
Minimum - Maximum-0.1794026 - 0.43435553
Average (Standard dev.)0.000043824108 (±0.012096659)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 328.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: half even map

Fileemd_61095_half_map_1.map
Annotationhalf even map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: half odd map

Fileemd_61095_half_map_2.map
Annotationhalf odd map
Projections & Slices
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Sample components

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Entire : Photosynthetic LH1-RC complex of Blastochloris tepida

EntireName: Photosynthetic LH1-RC complex of Blastochloris tepida
Components
  • Complex: Photosynthetic LH1-RC complex of Blastochloris tepida
    • Protein or peptide: Photosynthetic reaction center cytochrome c subunit
    • Protein or peptide: Reaction center protein L chain
    • Protein or peptide: Reaction center protein M chain
    • Protein or peptide: Photosynthetic reaction center subunit H
    • Protein or peptide: Antenna complex alpha/beta subunit domain-containing protein
    • Protein or peptide: Light-harvesting protein gamma1
    • Protein or peptide: Light-harvesting protein B-1015 gamma chain
    • Protein or peptide: Antenna complex alpha/beta subunit domain-containing protein
  • Ligand: HEME C
  • Ligand: MAGNESIUM ION
  • Ligand: Ubiquinone-8
  • Ligand: DIACYL GLYCEROL
  • Ligand: BACTERIOCHLOROPHYLL B
  • Ligand: BACTERIOPHEOPHYTIN B
  • Ligand: CARDIOLIPIN
  • Ligand: FE (III) ION
  • Ligand: MENAQUINONE-7
  • Ligand: 15-cis-1,2-dihydroneurosporene
  • Ligand: DODECYL-BETA-D-MALTOSIDE
  • Ligand: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE
  • Ligand: all-trans-1,2-dihydroneurosporene
  • Ligand: water

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Supramolecule #1: Photosynthetic LH1-RC complex of Blastochloris tepida

SupramoleculeName: Photosynthetic LH1-RC complex of Blastochloris tepida / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5, #7-#8, #6
Source (natural)Organism: Blastochloris tepida (bacteria)

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Macromolecule #1: Photosynthetic reaction center cytochrome c subunit

MacromoleculeName: Photosynthetic reaction center cytochrome c subunit / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Blastochloris tepida (bacteria)
Molecular weightTheoretical: 39.181129 KDa
SequenceString: MKHMIAKSVA TVALASLVSG CFEPPPAIST QTGFRGLSMG EVLHPATVAA KKERDAQYPP ALPAVKAEGQ PVSKVYKNVK VLGDLTEPE FLRTMTAMTE WVSPKEGCTY CHDEADLSSE AKYPFKVARR MLEMTRHINT DWTSHVAQTG VTCYTCHRGR P VPPYIRYL ...String:
MKHMIAKSVA TVALASLVSG CFEPPPAIST QTGFRGLSMG EVLHPATVAA KKERDAQYPP ALPAVKAEGQ PVSKVYKNVK VLGDLTEPE FLRTMTAMTE WVSPKEGCTY CHDEADLSSE AKYPFKVARR MLEMTRHINT DWTSHVAQTG VTCYTCHRGR P VPPYIRYL EPRLPLDNAI KPTFVEADNS GHVVRLAKNT AYSALNYDPF AMFLANDKRE IRFVPQTALP PVGVSRGMER RP LSDAYAT FALMMFISDA IGTNCTFCHN PQTFESWGNK STPQRAIAWQ GIKMTRDLNM NFLSPLKPVY PANRLGAQGE APM ADCRTC HQGVTKPLFG ASRMKDYPEL GPVKAAAK

UniProtKB: Photosynthetic reaction center cytochrome c subunit

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Macromolecule #2: Reaction center protein L chain

MacromoleculeName: Reaction center protein L chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Blastochloris tepida (bacteria)
Molecular weightTheoretical: 30.406064 KDa
SequenceString: MALLSFERKY RVRGGTLIGG DLFDFWVGPF YVGFFGVSAI FFIFLGVSLI GYAASQGPSL DPFAISINPP DLKYGFAGAP LLEGGFWQA ITVCAIGAFI SWQLREVEIS RKLGMGWHVP IAFGVPIFMF LVLQVFRPIL MGGWGFAFPY GILSHLDWVN N FGFQYLNW ...String:
MALLSFERKY RVRGGTLIGG DLFDFWVGPF YVGFFGVSAI FFIFLGVSLI GYAASQGPSL DPFAISINPP DLKYGFAGAP LLEGGFWQA ITVCAIGAFI SWQLREVEIS RKLGMGWHVP IAFGVPIFMF LVLQVFRPIL MGGWGFAFPY GILSHLDWVN N FGFQYLNW HYNPGHMSSV SFLFANAMAL GLHGGLILSV ANPGDGDKVK TAEHENAYFR DVVGYSIGAL AIHRLGLFLA SN IFLTGAF GTIASGPFWT RGWPEWWGWW LDIPFWS

UniProtKB: Reaction center protein L chain

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Macromolecule #3: Reaction center protein M chain

MacromoleculeName: Reaction center protein M chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Blastochloris tepida (bacteria)
Molecular weightTheoretical: 37.06877 KDa
SequenceString: MADFQTIYTQ IQARGPDHFG PSGQWGDIDR VGKPIFIKWL GRIGDAQIGP VYLGASGVGG IAFGLTAILI IGFNMLAQVS FDPLQFFRQ FFWLGLYPPK AQYGMGIPPL NDGGWWLMAG LMMTLSLGCW WIRVYSRARA LGLGTHIAWN FAMAIFFVLC I GFFHPVLV ...String:
MADFQTIYTQ IQARGPDHFG PSGQWGDIDR VGKPIFIKWL GRIGDAQIGP VYLGASGVGG IAFGLTAILI IGFNMLAQVS FDPLQFFRQ FFWLGLYPPK AQYGMGIPPL NDGGWWLMAG LMMTLSLGCW WIRVYSRARA LGLGTHIAWN FAMAIFFVLC I GFFHPVLV GSWSEAVPFG IFPHLDWLTA FSMRYGNFYY CPWHGFSIGF AYGCGLLFAA HGATILAVAR FGGDREIEQI TD RGTAVER AALFWRWTMG FNATIESIHR WGWFFSFMVM FSASVGILLT GTFVDNWYLW CVKHGAAPDY PAFLPATPDP RAG TFDPRT LTGVPQ

UniProtKB: Reaction center protein M chain

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Macromolecule #4: Photosynthetic reaction center subunit H

MacromoleculeName: Photosynthetic reaction center subunit H / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Blastochloris tepida (bacteria)
Molecular weightTheoretical: 28.839578 KDa
SequenceString: (FME)YYGALANHL DIAQLAWYGH WLVIWTVVLF YLRREDRREG YPLVEPLGLV KLPSPDVQSG ELPYPKTFTL YHGGTV QAP NPNRRYETRE LKLAQTDGFE GAPLAPTGNP MVDGVGPASW AERSEVVDST FEGKAKIVPL RAAPEFYIAE GDLDPRG LP VFGADGIEAG ...String:
(FME)YYGALANHL DIAQLAWYGH WLVIWTVVLF YLRREDRREG YPLVEPLGLV KLPSPDVQSG ELPYPKTFTL YHGGTV QAP NPNRRYETRE LKLAQTDGFE GAPLAPTGNP MVDGVGPASW AERSEVVDST FEGKAKIVPL RAAPEFYIAE GDLDPRG LP VFGADGIEAG TVTDLWVDRS EYYFRYLEIS VAGSARTALM PLGFASITKD GVKVQAILAS QFANVPRLQS RDQITLRE E DKVSAYYAGG LLYATPERAE PLL

UniProtKB: Photosynthetic reaction center subunit H

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Macromolecule #5: Antenna complex alpha/beta subunit domain-containing protein

MacromoleculeName: Antenna complex alpha/beta subunit domain-containing protein
type: protein_or_peptide / ID: 5 / Number of copies: 17 / Enantiomer: LEVO
Source (natural)Organism: Blastochloris tepida (bacteria)
Molecular weightTheoretical: 7.83426 KDa
SequenceString:
MANENPRSAS WKLWLILDPR RVLTALFIYL TVIALLIHFG LLSTNRLNWW EFQRGLPAAS LVVVPPAVG

UniProtKB: Antenna complex alpha/beta subunit domain-containing protein

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Macromolecule #6: Antenna complex alpha/beta subunit domain-containing protein

MacromoleculeName: Antenna complex alpha/beta subunit domain-containing protein
type: protein_or_peptide / ID: 6 / Number of copies: 17 / Enantiomer: LEVO
Source (natural)Organism: Blastochloris tepida (bacteria)
Molecular weightTheoretical: 7.653907 KDa
SequenceString:
MADLKPSLTG LTEEEAKEFH SVFVSSMVLY LATAVIVHYL VWTARPWIAP IPKGWVNLDG VTTALSYLV

UniProtKB: Antenna complex alpha/beta subunit domain-containing protein

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Macromolecule #7: Light-harvesting protein gamma1

MacromoleculeName: Light-harvesting protein gamma1 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Blastochloris tepida (bacteria)
Molecular weightTheoretical: 5.927073 KDa
SequenceString:
MKLSFVIGAL SAILASTAAS AAMVNGVVQP SITDWNLWVP LGILGIPTIW IALLYR

UniProtKB: Uncharacterized protein

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Macromolecule #8: Light-harvesting protein B-1015 gamma chain

MacromoleculeName: Light-harvesting protein B-1015 gamma chain / type: protein_or_peptide / ID: 8 / Number of copies: 15 / Enantiomer: LEVO
Source (natural)Organism: Blastochloris tepida (bacteria)
Molecular weightTheoretical: 5.93301 KDa
SequenceString:
MKLSAVIGAL SVVLTSTLAS AYFAADGSVV PSITDANLWV PLGILGIPTI WIALLYR

UniProtKB: Light-harvesting protein B-1015 gamma chain

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Macromolecule #9: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 9 / Number of copies: 4 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C

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Macromolecule #10: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 10 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #11: Ubiquinone-8

MacromoleculeName: Ubiquinone-8 / type: ligand / ID: 11 / Number of copies: 5 / Formula: UQ8
Molecular weightTheoretical: 727.109 Da
Chemical component information

ChemComp-UQ8:
Ubiquinone-8

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Macromolecule #12: DIACYL GLYCEROL

MacromoleculeName: DIACYL GLYCEROL / type: ligand / ID: 12 / Number of copies: 1 / Formula: DGA
Molecular weightTheoretical: 625.018 Da
Chemical component information

ChemComp-DGA:
DIACYL GLYCEROL

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Macromolecule #13: BACTERIOCHLOROPHYLL B

MacromoleculeName: BACTERIOCHLOROPHYLL B / type: ligand / ID: 13 / Number of copies: 38 / Formula: BCB
Molecular weightTheoretical: 909.488 Da
Chemical component information

ChemComp-BCB:
BACTERIOCHLOROPHYLL B

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Macromolecule #14: BACTERIOPHEOPHYTIN B

MacromoleculeName: BACTERIOPHEOPHYTIN B / type: ligand / ID: 14 / Number of copies: 2 / Formula: BPB
Molecular weightTheoretical: 887.199 Da
Chemical component information

ChemComp-BPB:
BACTERIOPHEOPHYTIN B

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Macromolecule #15: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 15 / Number of copies: 5 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

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Macromolecule #16: FE (III) ION

MacromoleculeName: FE (III) ION / type: ligand / ID: 16 / Number of copies: 1 / Formula: FE
Molecular weightTheoretical: 55.845 Da

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Macromolecule #17: MENAQUINONE-7

MacromoleculeName: MENAQUINONE-7 / type: ligand / ID: 17 / Number of copies: 1 / Formula: MQ7
Molecular weightTheoretical: 648.999 Da
Chemical component information

ChemComp-MQ7:
MENAQUINONE-7

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Macromolecule #18: 15-cis-1,2-dihydroneurosporene

MacromoleculeName: 15-cis-1,2-dihydroneurosporene / type: ligand / ID: 18 / Number of copies: 1 / Formula: NS5
Molecular weightTheoretical: 540.904 Da
Chemical component information

ChemComp-NS5:
15-cis-1,2-dihydroneurosporene

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Macromolecule #19: DODECYL-BETA-D-MALTOSIDE

MacromoleculeName: DODECYL-BETA-D-MALTOSIDE / type: ligand / ID: 19 / Number of copies: 8 / Formula: LMT
Molecular weightTheoretical: 510.615 Da
Chemical component information

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

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Macromolecule #20: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...

MacromoleculeName: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE
type: ligand / ID: 20 / Number of copies: 6 / Formula: PGV
Molecular weightTheoretical: 749.007 Da
Chemical component information

ChemComp-PGV:
(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / phospholipid*YM

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Macromolecule #21: all-trans-1,2-dihydroneurosporene

MacromoleculeName: all-trans-1,2-dihydroneurosporene / type: ligand / ID: 21 / Number of copies: 16 / Formula: NS0
Molecular weightTheoretical: 540.904 Da
Chemical component information

ChemComp-NS0:
all-trans-1,2-dihydroneurosporene

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Macromolecule #22: water

MacromoleculeName: water / type: ligand / ID: 22 / Number of copies: 423 / 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

Concentration3.8 mg/mL
BufferpH: 8.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.7 µm / Nominal defocus min: 0.9 µm
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: 373104
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 2.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 294012
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9j2f:
Structure of photosynthetic LH1-RC complex from the purple bacterium Blastochloris tepida

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