{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4c.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4a.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4b.xlsx"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4c_QE_Aur30min_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4b_QE_AurTS25_1hr_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4b_QE_AurTS25_1hr_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4c_QE_Aur30min_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4a_QE_Aur30min_WT-AV1-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4b_QE_AurTS25_1hr_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4a_QE_Aur30min_DJ605-AV1-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4b_QE_AurTS25_1hr_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD062624/Supplemental_Table_4a_QE_Aur30min_HpH-AV1-3.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["tfchou@caltech.edu"],"submitter":["Ting-Yu Wang"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Visual proteomics","Cryoet","Nitrogen fixation","Anerobic","Cryoem"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062624"],"sample_protocol":["All protein samples were incubated with 7.5 M urea for 15 min at 37 °C, then reduced with 4 mM TCEP for 20 min at 37 °C. Chloroacetamide was added to a final concentration of 12 mM and the samples were incubated for 15 min at 37 °C. 1.5 ng/μL endoproteinase LysC was added and the digestion proceeded for 1 hour at 37 °C. Samples were diluted to 2 M urea with 50 mM HEPES, (pH 8.0) and a final concentration of 1 mM CaCl2 final concentration was added. Trypsin was added at a concentration of 0.5 ng/μL and incubated overnight at 37 °C. Samples were desalted using Pierce™ C18 Spin Tips & Columns (ThermoFisher Scientific, product #89870). After desalting and drying, peptides were suspended in water containing 0.2% formic acid and 2% acetonitrile for further LC-MS/MS analysis. LC-MS/MS analysis was performed with an EASY-nLC 1200 (ThermoFisher Scientific, San Jose, CA) coupled to a Q Exactive HF hybrid quadrupole-Orbitrap mass spectrometer (ThermoFisher Scientific, San Jose, CA). Peptides were separated on an Aurora UHPLC Column (25 cm × 75 μm, 1.6 μm C18, AUR2-25075C18A, Ion Opticks) with a flow rate of 0.35 μL/min for a total duration of 75 min and ionized at 1.6 kV in the positive ion mode. The gradient was composed of 6% solvent B (2 min), 6-25% B (20.5 min), 25-40% B (7.5 min), and 40–98% B (13 min); solvent A: 2% acetonitrile (ACN) and 0.2% formic acid (FA) in water; solvent B: 80% ACN and 0.2% FA. MS1 scans were acquired at the resolution of 60,000 from 375 to 1500 m/z, AGC target 3e6, and maximum injection time 15 ms. The 12 most abundant ions in MS2 scans were acquired at a resolution of 30,000, AGC target 1e5, maximum injection time 60 ms, and normalized collision energy of 28. Dynamic exclusion was set to 30 s and ions with charge +1, +7, +8 and >+8 were excluded. The temperature of ion transfer tube was 275 °C and the S-lens RF level was set to 60."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS2 fragmentation spectra were searched with Proteome Discoverer SEQUEST (version 2.5, Thermo Scientific) against in silico tryptic digested Uniprot all-reviewed Azotobacter vinelandii database. The maximum missed cleavages were set to 2. Dynamic modifications were set to oxidation on methionine (M, +15.995 Da), deamidation on asparagine and glutamine (N and Q, +0.984 Da) and protein N-terminal acetylation (+42.011 Da). The maximum parental mass error was set to 10 ppm, and the MS2 mass tolerance was set to 0.03 Da. The false discovery threshold was set strictly to 0.01 using the Percolator Node validated by q-value. The relative abundance of parental peptides was calculated by integration of the area under the curve of the MS1 peaks using the Minora LFQ node."],"omics_type":["Proteomics"],"labhead":["Tsui-Fen Chou"],"instrument_platform":[""],"labhead_affiliation":["Proteome Exploration Laboratory, California Institute of Technology, Pasadena, CA, USA"],"submission_type":["PARTIAL"],"species":["Bacteria","Azotobacter Vinelandii"],"publication":["40664216 Shen Y, Maggiolo AO, Zhang T, Warmack RA. CryoEM-enabled visual proteomics reveals de novo structures of oligomeric protein complexes. Structure. 2025 33(9):1484-1497.e5 10.1016/j.str.2025.06.007"],"submitter_mail":["tywang@caltech.edu"],"submitter_affiliation":["Caltech"],"submitter_country":["United States"],"pubmed_abstract":["Single particle cryoelectron microscopy (cryoEM) and cryoelectron tomography (cryoET) are powerful methods for unveiling unique and functionally relevant structural states. Aided by mass spectrometry and machine learning, they promise to facilitate the visual exploration of proteomes. Leveraging visual proteomics, we interrogate structures isolated from a complex cellular milieu by cryoEM to identify and classify molecular structures and complexes de novo. By comparing three automated model building programs, CryoID, DeepTracer, and ModelAngelo, we determine the identity of six distinct oligomeric protein complexes from partially purified extracts of the nitrogen-fixing bacterium Azotobacter vinelandii using both anaerobic and aerobic cryoEM, including two original oligomeric structures. Overall, by allowing the study of near-native oligomeric protein states, cryoEM-enabled visual proteomics reveals unique structures that correspond to relevant species observed in situ."],"pubmed_title":["CryoEM-enabled visual proteomics reveals de novo structures of oligomeric protein complexes."],"pubmed_authors":["Shen Yuanbo Y, Maggiolo Ailiena O AO, Zhang Tianzheng T, Warmack Rebeccah A RA"],"additional_accession":[]},"is_claimable":false,"name":"CryoEM-enabled visual proteomics reveals de novo structures of oligomeric protein complexes from Azotobacter vinelandii","description":"Single particle cryoelectron microscopy (cryoEM) and cryoelectron tomography (cryoET) are powerful methods for unveiling unique and functionally relevant structural states. Aided by mass spectrometry and machine learning, they promise to facilitate the visual exploration of proteomes. Leveraging visual proteomics, we interrogate structures isolated from a complex cellular milieu by cryoEM to identify and classify molecular structures and complexes de novo. That approach determines the identity of six distinct oligomeric protein complexes from partially purified extracts of Azotobacter vinelandii using both anaerobic and aerobic cryoEM. Identification of the first unknown species, phosphoglucoisomerase (Pgi1), is achieved by comparing three automated model building programs: CryoID, DeepTracer, and ModelAngelo with or without a priori proteomics data. All three programs identify the Pgi1 protein, revealed to be in a new decameric state, as well as additional globular structures identified as glutamine synthetase (GlnA) and bacterioferritin (Bfr). Large filamentous assemblies are observed in tomograms reconstructed from cryoFIB milled lamellae of nitrogen-fixing A. vinelandii. Enrichment of these species from the cells by centrifugation allows for structure determination of three distinct filament types by helical reconstruction methods: the Type 6 Secretion System non-contractile sheath tube (TssC), a novel filamentous form of the soluble pyridine transhydrogenase (SthA), and the flagellar filament (FliC). The multimeric states of Pgi1 and SthA stand out in contrast to known crystallographic structures and offer a new structural framework from which to evaluate their activities. Overall, by allowing the study of near-native oligomeric protein states, cryoEM-enabled visual proteomics reveals novel structures that correspond to relevant species observed in 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