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FANG"],"technology_type":["Mass Spectrometry","Top-down proteomics"],"software":[""],"submitter_keywords":["Topology characterization","Surface-induced dissociation","Protein complex identification","Native proteomics","Capillary electrophoresis-mass spectrometry"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069439"],"sample_protocol":["Sample preparation E. coli (strain Top10  ) was cultured in Terrific Broth (TB) medium at 37 °C with shaking until the optical density at 600 nm (OD600) reached 0.77. The bacterial cells were then washed three times with DPBS and pelleted by centrifugation. A 0.45 g pellet was resuspended in 1.6 mL DPBS supplemented with cOmplete protease inhibitors and phosphatase inhibitors (1%, w/v) and homogenized for 30 seconds three times using homogenizer 150 (Fisher Scientific) and subsequently sonicated on ice using a Branson Sonifier 250 (VWR Scientific, Batavia, IL) for 2 minutes, repeated 6 times. The lysate was centrifuged at 16,000 × g for 20 minutes at 4°C, and the resulting supernatant was collected. Protein concentration (~6 mg/mL) was determined using the bicinchoninic acid (BCA) assay (Fisher Scientific). Size-exclusion chromatography (SEC) fractionation Lysates were subsequently injected (20 μL per injection) into an Agilent Infinity II HPLC system equipped with an Agilent Bio SEC-5 column (4.6 × 300 mm, 5 µm particle size, 500 Å pore size) from Agilent Technologies (Santa Clara, CA). The mobile phase was 100 mM NH4Ac, pH 7) at a flow rate of 0.2 mL/min. Fractions were collected every minute from 8.5 min to 23.5 min, while the sample was collected from 23.5-27 min as one fraction, yielding a total of 16 fractions. Corresponding fractions from 16 replicates were combined and concentrated using Amicon-30 kDa centrifugal filter units. The buffer was exchanged by washing twice with 20 mM NH4Ac (pH 6.9). The proteins were collected, and the concentration was measured using the BCA assay. The recovered protein samples were frozen in -80 °C until analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For  the nCZE-MS and nCZE-MS/MS data, manual integration on the electropherograms was performed for each fraction to generate its corresponding mass spectra. Mass spectra were either deconvolved manually or using Unidec.25 The processed masses were compiled into Table S3. Target masses were generated by inputting the IDs from the bottom-up experiments into the ID mapping function from UniProt, and the output was input into ProSight Native as the target database. HCD/SID-generated monomer masses were batch added to the complex-down function in ProSight Native for database searching. Higher-order oligomers were assigned based on the integer multiple of the monomer mass, based on the observed oligomeric state from the protein data bank.  For all the TDP mass spectra obtained with high-high mode, proteoform identification from E. coli lysate was performed using TopPIC (Top-down mass spectrometry-based Proteoform Identification and Characterization) pipelines. Briefly, the raw file was converted to mzML files by MSConvert using the peak-picking algorithm. Then, the spectral deconvolution was performed using Top-down mass spectrometry Feature Detection (TopFD, version 1.6.3) with default parameters. The database search was performed using TopPIC (1.6.3) against the UniProt proteome database of E. coli (UP000002311, 4602 entries, accessed on 04/11/2025). The parameters were set as follows: mass error tolerance of matching masses of 10 ppm, maximum number of variable modifications (including acetylation, phosphorylation, oxidation, and methylation) of 3, maximum number of mass shifts of unknown modification of 2, ranging from -500 Da to 500 Da. The false discovery rates (FDRs) were estimated using the target-decoy approach. The spectrum level FDR cutoff was 1%, and the proteoform level FDR cutoff was 1%.  For complex samples analyzed by low-high mode, the raw files were first converted to mzML files by MSConvert using a peak-picking algorithm. Then, the spectral deconvolution was performed using TopFD, version 1.6.3, with the default parameters except that the maximum charge setting was 100, the maximum mass was 100,000 Da and enable Missing MS1 spectra. Then, the obtained MSAlign files were processed using ProSight Lite software.  For the bottom-up experiment, the raw files were processed using SEQUEST integrated in Proteome Discoverer 2.2. The MS/MS spectra were searched against the UniProt Ecoli proteome database (UniProt-proteome_UP00000625, 4588 entries, accessed on 04/17/2025). The search parameters were specified as: precursor mass tolerance was 20 ppm; fragment mass tolerance was 0.02 Da. The maximum missed cleavages per peptide was 2. Carbamidomethylation of cysteine residues (+57.0215 Da) was set as a fixed modification. Acetyl (+42.011 Da(N-Terminus)) was set as a dynamic modification on the N-terminal of the protein. Oxidation (+15.995 Da(M)) and deamidation (+0.984 Da (N, Q)) were set as dynamic modifications. The target FDR of the decoy database search was set as 0.01."],"omics_type":["Proteomics"],"labhead":["Liangliang Sun"],"instrument_platform":[""],"labhead_affiliation":["Michigan State University"],"submission_type":["PARTIAL"],"species":["Escherichia Coli"],"publication":["10.1021/ACS.ANALCHEM.6C01693"],"submitter_mail":["fiona.dicp@outlook.com"],"submitter_affiliation":["Michigan State University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Multi-dimensional native proteomics technology for protein complex identification and topology characterization (Mud-NatPIT)","description":"Here, we demonstrate a pilot development of multi-dimensional native proteomics technology for protein complex identification and topology characterization (Mud-NatPIT) in complex biological samples via coupling native size exclusion chromatography (SEC), online native capillary electrophoresis-mass spectrometry (nCE-MS), surface-induced dissociation (SID), and multi-level proteomics. The Mud-NatPIT enabled the detection of 124 unique native endogenous protein complexes with masses up to 1.5 MDa from a whole cell lysate, identified 46 unique protein complexes in a discovery mode, and provided topological information for 39 protein complexes. The Mud-NatPIT is broadly applicable for characterizing protein complexes in cells, tissues, and biological fluids.","dates":{"publication":"2026-08-04","submission":"2025-10-14"},"accession":"PXD069439","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:510516","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NE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