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After stratification at 4°C for 3 days, the plates were transferred to growth conditions. Plants were vertically grown in a growth chamber at 22°C under a 16-hour light / 8-hour dark cycle for 12 days, then flash frozen in liquid nitrogen and stored at -80°C for crosslinking.Frozen Arabidopsis tissue was cryo-ground to a fine powder. A total 195 grams of tissue from 12d seedling were used for the chloroplast cross-linking experiment. Fraction of plant seedling tissues and isolation of intact chloroplast Chloroplast isolation: Frozen, homogenized tissue powder from 12 d old seedlings was mixed with a grinding buffer. Briefly, every 5 g of tissue powder was ground in a mortar and pestle with 30ml of grinding buffer [20mM HEPES-KOH pH 8.0, 330mM sorbitol, 5 mM EDTA, 5 mM EGTA, 5 mM MgCl2, and 10 mM NaHCO3] at 4°C, and under green illumination only. The resuspended homogenate was filtered twice through two layers of Miracloth. 30 ml of the filtrate was carefully transferred onto 10 ml of 40% Percoll [20 mM HEPES-KOH pH 8.0, 330 mM sorbitol, 40% v/v Percoll, 2.5 mM EDTA, 5 mM MgCl2, and 10 mM NaHCO3] in a 50ml centrifuge tube, and centrifuged at 2,600g for 10 min at 4°C. The bottom pellet, enriched in intact chloroplasts, was collected and resuspended in 30 ml of wash buffer [20 mM HEPES-KOH pH 8.0, 330 mM sorbitol, 2.5 mM EDTA, 2 mM MgCl2, and 10 mM NaHCO3], and centrifuged at 2,600g for 3 min at 4°C. Each pellet derived from 5 g of tissue was washed twice with 4.5 ml of 1x PBS supplemented with MgCl2 [137 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, and 2.5 mM MgCl2] and then resuspended in 1mL 1x PBS supplemented with MgCl2 for the cross-linking reaction. This process was repeated across multiple batches, with a total of 195 g of tissue used for cross-linking. Cross-linking reaction PhoX cross-linker was freshly prepared at a stock concentration of 100 mM in DMSO for each cross-linking experiment. A working concentration of 2-5 mM cross-linker was added to the buffer solution containing isolated chloroplasts and incubated for 2 h at 4°C in the dark with end-to-end rotation. The cross-linking reaction was quenched by adding Tris pH 8.0 to a final concentration of 20 mM, and subjected to protein extraction. Protein extraction, digestion, IMAC enrichment and high pH reverse-phase HPLC fractionation  Protein extraction from the cross-linked samples, digestion to peptides, immobilized metal affinity chromatography (IMAC) enrichment, and high pH reverse HPLC fractionation followed the same procedure as described in Xu et al (DOI: 10.1073/pnas.1610452114). Multiple batches of PhoX-cross-linked peptides from isolated intact chloroplasts were combined before IMAC enrichment. Multiple batches of samples were combined prior to high pH reverse HPLC fractionation. To generate a selective chloroplast proteomic database, total peptides from chloroplast samples were fractionated into eight fractions using the Pierce High pH Reverse-Phase Peptide Fractionation Kit and analyzed by LC-MS/MS."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["LC-MS/MS analysis Cross-linked peptides were analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) using an Easy-nLC 1200 ultra-performance liquid chromatography (UPLC) system (Thermo Fisher) coupled to an Orbitrap Eclipse Tribrid quadrupole Orbitrap mass spectrometer (Thermo Fisher). Peptides were first loaded onto a C18 trap column (Acclaim PepMap 100 C18) and then separated on an analytical C18 column (Aurora Series, 25 cm × 75 µm ID, Ion Opticks). The flow rate was set to 300 nL/min and the separation was performed over a 120-minute gradient. Peptides were eluted using a gradient from 3% to 28% solvent B over 106 minutes, followed by an increase from 28% to 44% over 15 minutes and a final wash at 90% solvent B for 14 minutes. Solvent A consisted of 0.1% formic acid and solvent B consisted of 80% (v/v) acetonitrile with 0.1% (v/v) formic acid.Data was acquired on an Orbitrap Eclipse mass spectrometer. Full MS scans were acquired over a mass-to-charge (m/z) range of 375–1600 at a resolution of 120,000, with an automatic gain control (AGC) target of 200,000, a maximum injection time of 50 ms, normalized AGC target set to 50%, and RF lens set to 30%. The most intense multiply charged precursors (charge states 2–8) were selected for fragmentation with a cycle time of 3 seconds. MS/MS scans were acquired at a resolution of 15,000 with an AGC target of 5 × 10⁴, maximum injection time of 22 ms, isolation window of 1.4 m/z, and normalized AGC target set to 100%. Fragmentation was performed using higher-energy collisional dissociation (HCD) with a normalized collision energy (NCE) of 27. Dynamic exclusion was enabled for 30 seconds. For cross-linked peptide detection, charge states from 3 to 8 were used.Data search using pLINK2 and Protein Prospector  Linear peptides were searched against the Arabidopsis TAIR database using Protein Prospector as described in (doi: 10.3389/fpls.2022.832562), and with Fragpipe. Phosphopeptide searches were analyzed using FragPipe. Precursor and fragment mass tolerance were set up as 10 and 20 ppm. Crosslinked peptide searches were performed using pLink3.2 (unreleased version). The pLink3 framework (https://github.com/pFindStudio/pLink3) incorporates multiple machine learning-driven scoring algorithms, a novel indexing structure, and high-level FDR control, providing comprehensive end-to-end optimization over pLink2 {Chen, 2019 #123}. Version 3.2 further extends pLink3.0 by unifying non-cleavable and cleavable cross-linkers within a single hierarchical funnel architecture. Crosslinked peptide searches were performed using pLink 3.2.0 with the following parameters: crosslinker set to PhoX (cross-linked mass: 209.972 Da; mono-linked mass: 227.982 Da); peptide length range: 6-60 amino acids; peptide mass range 600-6000 Da; enzyme: trypsin with up to 3 missed cleavages. Fixed modification: Cys carbamidomethylation; variable modifications: protein N-terminal acetylation and Met oxidation. Precursor and fragment mass tolerances were set to 5 ppm and 20 ppm, respectively.MS2 spectra were searched against compartment-specific databases for chloroplast (9798 entries). Results were filtered at 1% FDR at the peptide pair level. FDRs for monolinks, loop-links, intra- and inter-protein cross-links were calculated separately by pLINK3.2."],"omics_type":["Proteomics"],"labhead":["shouling xu"],"instrument_platform":[""],"labhead_affiliation":["Carnegie Mass Spectrometry Facility"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"submission_type":["PARTIAL"],"publication":["Not available"],"submitter_mail":["sxu@ciw.edu"],"submitter_affiliation":["Carnegie Institution at Stanford"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Mapping Architecture of Protein complexes in Arabidopsis using XL-MS (Part II Chloroplast)","description":"Capturing molecular machines in action is key to understanding protein complex architecture, cellular regulation, and gene function. Here, we present a cross-linking mass spectrometry (XL-MS) platform using the PhoX cross-linker to map proteome-wide interactions in Arabidopsis thaliana. By analyzing whole-cell lysates, chloroplasts, and nuclei, we identified 52,944 unique cross-links pairs, corresponding to 37,531 residue pairs captured across 5,064 proteins and 3,083 protein-protein interactions (2,385 heteromeric and 698 homomultimeric). Comparison with the STRING database showed that 676 interactions had scores ≥ 0.9 and 241 ranged from 0.7–0.9. Our dataset provides residue-level interfaces that complement existing interaction networks with experimental evidence of spatial proximity. XL-MS captured the spatial organization of protein complexes, including the chloroplast 70S ribosome stalk and intermediates in photosystem repair, and revealed both shared and distinct interaction patterns across photosystems, ribosomes, and chromatin-associated proteins. The data also suggest ribosome ubiquitination, supported by diGly proteomics, and are consistent with histone interaction patterns observed using histone-TurboID. In addition, we identified an O-acyltransferase associated with histones, suggesting a potential role in chromatin-related processes. Together, these results demonstrate the utility of XL-MS for system-level mapping of the plant proteome and provide a resource for further study. 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