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Open data
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Basic information
| Entry | ![]() | ||||||||||||||||||
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| Title | Photosystem II from Arabidopsis thaliana | ||||||||||||||||||
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Keywords | Membrane bound / Photosystem II / Arabidopsis / Manganese cluster / oxidoreductase / PHOTOSYNTHESIS | ||||||||||||||||||
| Function / homology | Function and homology informationresponse to desiccation / cellular response to water deprivation / photosystem I assembly / nonphotochemical quenching / chloroplast photosystem II / photoinhibition / photosynthesis, light harvesting in photosystem II / photosystem II antenna complex / response to red light / cellular response to abscisic acid stimulus ...response to desiccation / cellular response to water deprivation / photosystem I assembly / nonphotochemical quenching / chloroplast photosystem II / photoinhibition / photosynthesis, light harvesting in photosystem II / photosystem II antenna complex / response to red light / cellular response to abscisic acid stimulus / PSII associated light-harvesting complex II / chloroplast stromal thylakoid / response to low light intensity stimulus / thylakoid lumen / plastid thylakoid membrane / plastoglobule / salicylic acid binding / regulation of stomatal closure / response to far red light / thylakoid membrane / response to high light intensity / chloroplast thylakoid / photosynthesis, light harvesting in photosystem I / photosystem II oxygen evolving complex / photosystem II assembly / chloroplast thylakoid lumen / apoplast / thylakoid / oxygen evolving activity / photosystem II stabilization / protein phosphatase regulator activity / photosystem II reaction center / photosystem II / chloroplast envelope / photosynthetic electron transport chain / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / photosystem I / photosystem II / response to herbicide / extrinsic component of membrane / poly(U) RNA binding / chloroplast stroma / plastid / photosynthetic electron transport in photosystem II / positive regulation of reactive oxygen species biosynthetic process / chlorophyll binding / photosynthesis, light reaction / phosphate ion binding / chloroplast thylakoid membrane / response to light stimulus / response to cold / photosynthesis / chloroplast / electron transfer activity / protein stabilization / iron ion binding / protein domain specific binding / mRNA binding / heme binding / calcium ion binding / mitochondrion / extracellular region / metal ion binding / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.44 Å | ||||||||||||||||||
Authors | Forsman JA / Graca AT / Hussein R / Hall M / Messinger J / Schroder WP / Aydin AO | ||||||||||||||||||
| Funding support | Sweden, Germany, 5 items
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Citation | Journal: New Phytol / Year: 2026Title: The structure of intact and active Photosystem II from Arabidopsis thaliana at 2.44 Å resolution. Authors: Jack Forsman / André T Graça / Abuzer Orkun Aydin / Michael Hall / Rana Hussein / Wolfgang P Schröder / Johannes Messinger / ![]() Abstract: Photosystem II (PS II) is a large membrane-bound protein complex that catalyses light-driven water oxidation in plants and cyanobacteria. The structure of PS II is well studied in cyanobacteria; ...Photosystem II (PS II) is a large membrane-bound protein complex that catalyses light-driven water oxidation in plants and cyanobacteria. The structure of PS II is well studied in cyanobacteria; however, there are very few PS II structures from plants. The currently available plant PS II structures are comparatively low resolution and are frequently incomplete, that is, missing subunits or cofactors. We optimized the procedure for isolating PS II from Arabidopsis thaliana and employed cryo-electron microscopy to generate a high-resolution structure of an intact and oxygen-evolving PS II from Arabidopsis thaliana at 2.44 Å resolution, which to date represents the highest resolution structure of PS II from higher plants. At this resolution, many water molecules within the PS II structure can be detected, including waters around the water-splitting manganese cluster, the nonheme iron, and within the water/proton channels connecting these active sites to the protein exterior, allowing for the first detailed description of the water networks in Arabidopsis thaliana and comparison with the highly resolved cyanobacterial PS II. Our findings further the understanding of design principles of protein-water-cofactor interactions in photosynthetic water splitting, quinone reduction/exchange, and about the role of lipids at the interface between PS II and the light-harvesting proteins. | ||||||||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_52620.map.gz | 921.6 MB | EMDB map data format | |
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| Header (meta data) | emd-52620-v30.xml emd-52620.xml | 61.6 KB 61.6 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_52620_fsc.xml | 25.9 KB | Display | FSC data file |
| Images | emd_52620.png | 157.8 KB | ||
| Filedesc metadata | emd-52620.cif.gz | 12.1 KB | ||
| Others | emd_52620_additional_1.map.gz emd_52620_additional_2.map.gz emd_52620_half_map_1.map.gz emd_52620_half_map_2.map.gz | 49.8 MB 1.7 GB 1.7 GB 1.7 GB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-52620 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-52620 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9i4tMC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_52620.map.gz / Format: CCP4 / Size: 1.8 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
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| Voxel size | X=Y=Z: 0.7155 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: #2
| File | emd_52620_additional_1.map | ||||||||||||
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-Additional map: #1
| File | emd_52620_additional_2.map | ||||||||||||
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-Half map: #2
| File | emd_52620_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_52620_half_map_2.map | ||||||||||||
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Sample components
+Entire : C2S2-type Photosystem II complex from Arabidopsis thaliana
+Supramolecule #1: C2S2-type Photosystem II complex from Arabidopsis thaliana
+Macromolecule #1: Photosystem II protein D1
+Macromolecule #2: Photosystem II CP47 reaction center protein
+Macromolecule #3: Photosystem II CP43 reaction center protein
+Macromolecule #4: Photosystem II D2 protein
+Macromolecule #5: Cytochrome b559 subunit alpha
+Macromolecule #6: Cytochrome b559 subunit beta
+Macromolecule #7: Chlorophyll a-b binding protein 1, chloroplastic
+Macromolecule #8: Photosystem II reaction center protein H
+Macromolecule #9: Photosystem II reaction center protein I
+Macromolecule #10: Photosystem II reaction center protein J
+Macromolecule #11: Photosystem II reaction center protein K
+Macromolecule #12: Photosystem II reaction center protein L
+Macromolecule #13: Photosystem II reaction center protein M
+Macromolecule #14: Oxygen-evolving enhancer protein 1-1, chloroplastic
+Macromolecule #15: Oxygen-evolving enhancer protein 2-1, chloroplastic
+Macromolecule #16: Oxygen-evolving enhancer protein 3-1, chloroplastic
+Macromolecule #17: Chlorophyll a-b binding protein CP29.1, chloroplastic
+Macromolecule #18: Chlorophyll a-b binding protein CP26, chloroplastic
+Macromolecule #19: Photosystem II reaction center protein T
+Macromolecule #20: Photosystem II 5 kDa protein, chloroplastic
+Macromolecule #21: Photosystem II reaction center W protein, chloroplastic
+Macromolecule #22: Expressed protein
+Macromolecule #23: Chlorophyll a-b binding protein 2.1, chloroplastic
+Macromolecule #24: Photosystem II reaction center protein Z
+Macromolecule #25: CHLORIDE ION
+Macromolecule #26: CHLOROPHYLL A
+Macromolecule #27: PHEOPHYTIN A
+Macromolecule #28: BETA-CAROTENE
+Macromolecule #29: 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL
+Macromolecule #30: 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,...
+Macromolecule #31: FE (II) ION
+Macromolecule #32: BICARBONATE ION
+Macromolecule #33: DIGALACTOSYL DIACYL GLYCEROL (DGDG)
+Macromolecule #34: 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
+Macromolecule #35: CA-MN4-O5 CLUSTER
+Macromolecule #36: DODECYL-BETA-D-MALTOSIDE
+Macromolecule #37: 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
+Macromolecule #38: PROTOPORPHYRIN IX CONTAINING FE
+Macromolecule #39: CHLOROPHYLL B
+Macromolecule #40: (3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL
+Macromolecule #41: (3S,5R,6S,3'S,5'R,6'S)-5,6,5',6'-DIEPOXY-5,6,5',6'- TETRAHYDRO-BE...
+Macromolecule #42: (1R,3R)-6-{(3E,5E,7E,9E,11E,13E,15E,17E)-18-[(1S,4R,6R)-4-HYDROXY...
+Macromolecule #43: water
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 9.7 mg/mL | ||||||||||||||||||
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| Buffer | pH: 6 Component:
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| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Details: 50 mA | ||||||||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV | ||||||||||||||||||
| Details | Thylakoid membranes were solubilised using b-dodecylmaltoside. The C2S2-type Photosystem II complexes were isolated using sucrose gradients. |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Energy filter - Name: TFS Selectris / Energy filter - Slit width: 10 eV |
| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 16450 / Average exposure time: 2.17 sec. / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 165000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
Sweden,
Germany, 5 items
Citation




Z (Sec.)
Y (Row.)
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Processing
FIELD EMISSION GUN


