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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Cryo-EM structure of rice PHS1-DPE1 complex | |||||||||
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Sample |
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Keywords | Complex / Starch biosynthersis / Rice / Maltooligosaccharide elongation / TRANSFERASE | |||||||||
| Function / homology | Function and homology informationamyloplast / maltose catabolic process / 4-alpha-glucanotransferase / 4-alpha-glucanotransferase activity / starch catabolic process / glycogen phosphorylase / glycogen phosphorylase activity / polysaccharide catabolic process / chloroplast / glucose metabolic process ...amyloplast / maltose catabolic process / 4-alpha-glucanotransferase / 4-alpha-glucanotransferase activity / starch catabolic process / glycogen phosphorylase / glycogen phosphorylase activity / polysaccharide catabolic process / chloroplast / glucose metabolic process / pyridoxal phosphate binding / carbohydrate metabolic process Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / negative staining / Resolution: 2.78 Å | |||||||||
Authors | Jian L / Junjie Y | |||||||||
| Funding support | China, 2 items
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Citation | Journal: To Be PublishedTitle: Cryo-EM structure of rice PHS1-DPE1 complex protomer I Authors: Jian L / Junjie Y | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_63277.map.gz | 230 MB | EMDB map data format | |
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| Header (meta data) | emd-63277-v30.xml emd-63277.xml | 18 KB 18 KB | Display Display | EMDB header |
| Images | emd_63277.png | 84.2 KB | ||
| Filedesc metadata | emd-63277.cif.gz | 6.8 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-63277 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-63277 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9lpwMC C: citing same article ( M: atomic model generated by this map |
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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_63277.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.84 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : PHS1-DPE1 complex protomer I
| Entire | Name: PHS1-DPE1 complex protomer I |
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| Components |
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-Supramolecule #1: PHS1-DPE1 complex protomer I
| Supramolecule | Name: PHS1-DPE1 complex protomer I / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #2, #1 |
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| Source (natural) | Organism: ![]() Location in cell: chloroplast |
-Macromolecule #1: Alpha-1,4 glucan phosphorylase
| Macromolecule | Name: Alpha-1,4 glucan phosphorylase / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: glycogen phosphorylase |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 109.299164 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MATASAPLQL ATASRPLPVG VGCGGGGGGG LHVGGARGGG AAPARRRLAV RSVASDRGVQ GSVSPEEEIS SVLNSIDSST IASNIKHHA EFTPVFSPEH FSPLKAYHAT AKSVLDTLIM NWNATYDYYD RTNVKQAYYL SMEFLQGRAL TNAVGNLELT G QYAEALQQ ...String: MATASAPLQL ATASRPLPVG VGCGGGGGGG LHVGGARGGG AAPARRRLAV RSVASDRGVQ GSVSPEEEIS SVLNSIDSST IASNIKHHA EFTPVFSPEH FSPLKAYHAT AKSVLDTLIM NWNATYDYYD RTNVKQAYYL SMEFLQGRAL TNAVGNLELT G QYAEALQQ LGHSLEDVAT QEPDAALGNG GLGRLASCFL DSLATLNYPA WGYGLRYKHG LFKQIITKDG QEEVAENWLE MG NPWEIVR TDVSYPVKFY GKVVEGTDGR MHWIGGENIK VVAHDIPIPG YKTKTTNNLR LWSTTVPSQD FDLEAFNAGD HAS AYEAHL NAEKICHVLY PGDESPEGKV LRLKQQYTLC SASLQDIIAR FERRAGDSLS WEDFPSKVAV QMNDTHPTLC IPEL MRILI DVKGLSWNEA WSITERTVAY TNHTVLPEAL EKWSLDIMQK LLPRHVEIIE KIDGELMNII ISKYGTEDTS LLKKK IKEM RILDNIDLPD SIAKLFVKPK EKKESPAKLK EKLLVKSLEP SVVVEEKTVS KVEINEDSEE VEVDSEEVVE AENEDS EDE LDPFVKSDPK LPRVVRMANL CVVGGHSVNG VAAIHSEIVK EDVFNSFYEM WPAKFQNKTN GVTPRRWIRF CNPELSA II SKWIGSDDWV LNTDKLAELK KFADDEDLQS EWRAAKKANK VKVVSLIREK TGYIVSPDAM FDVQVKRIHE YKRQLLNI L GIVYRYKKMK EMSAKDRINS FVPRVCIFGG KAFATYVQAK RIVKFITDVA ATVNHDPEIG DLLKVVFIPD YNVSVAEAL IPASELSQHI STAGMEASGT SNMKFAMNGC ILIGTLDGAN VEIREEVGEE NFFLFGAEAH EIAGLRKERA QGKFVPDPRF EEVKRFVRS GVFGTYNYDD LMGSLEGNEG YGRADYFLVG KDFPSYIECQ EKVDKAYRDQ KLWTRMSILN TASSSKFNSD R TIHEYAKD IWDIKPVILP UniProtKB: Alpha-1,4 glucan phosphorylase |
-Macromolecule #2: 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
| Macromolecule | Name: 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO / EC number: 4-alpha-glucanotransferase |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 66.360562 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MATLSLPLPH LTQAIPARAR PRPRPLRGIP ARLLSCRAAM AVAPDKEEAA AVALDKAVKV AVAAPDRAAV AAVGVGEELP EGYDQMMPA VEEARRRRAG VLLHPTSLRG PHGIGDLGDE AVAFLAWLRD AGCTLWQVLP LVPPGRKSGE DGSPYSGQDA N CGNTLLIS ...String: MATLSLPLPH LTQAIPARAR PRPRPLRGIP ARLLSCRAAM AVAPDKEEAA AVALDKAVKV AVAAPDRAAV AAVGVGEELP EGYDQMMPA VEEARRRRAG VLLHPTSLRG PHGIGDLGDE AVAFLAWLRD AGCTLWQVLP LVPPGRKSGE DGSPYSGQDA N CGNTLLIS LEELVKDGLL MENELPDPLD MEYVEFDTVA NLKEPLIAKA AERLLLSRGE LRTQYDCFKK NPNISGWLED AA LFAAIDR SIDALSWYEW PEPLKNRHLR ALEDIYQKQK DFIEIFMAQQ FLFQRQWQRI RKYAKKLGIS IMGDMPIYVG YHS ADVWAN RKSFLLDKNG FPTFVSGVPP DAFSETGQLW NSPLYDWKAM EAGGFEWWIK RINRALDLYD EFRIDHFRGL AGFW AVPSE SKVALVGSWR AGPRNAFFDA LFKAVGRINI IAEDLGVITE DVVDLRKSIE APGMAVLQFA FGGGSDNPHL PHNHE FDQV VYTGTHDNDT VIGWWQTLPE EEKQTVFKYL PEANRTEISW ALITAALSSV ARTSMVTMQD ILGLDSSARM NTPATQ KGN WRWRMPSSVS FDSLSPEAAK LKELLGLYNR L UniProtKB: 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic |
-Experimental details
-Structure determination
| Method | negative staining, cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1.07 mg/mL | |||||||||
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| Buffer | pH: 8 Component:
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| Staining | Type: NEGATIVE / Material: Uranyl Acetate | |||||||||
| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec. / Details: 15 mA | |||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV | |||||||||
| Details | 1.07 mg/ml complex |
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Electron microscopy
| Microscope | FEI POLARA 300 |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 1160 / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: OTHER / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Tecnai Polara / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Protocol: AB INITIO MODEL |
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| Output model | ![]() PDB-9lpw: |
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About Yorodumi




Keywords
Authors
China, 2 items
Citation





Z (Sec.)
Y (Row.)
X (Col.)





















FIELD EMISSION GUN
