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Detailed conditions are in Supplementary Table 1. Four experimental conditions were set, the combination of At and So with PhoX 1 mM (P1) and 2 mM (P2), denominated as At_P1, At_P2, So_P1, So_P2. The reaction mix was kept in the dark at room temperature, and it was stopped after 30 minutes with 50 mM NH3. An extra step of thylakoid washing was performed in At_P1 and So_P1 to remove non-membrane proteins. These samples were centrifuged at 3000×g for 5 min, resuspended in 1 mL of only base buffer, and centrifuged again before final resuspension in 300 µL of fresh base buffer. Another crucial aspect is that P1 treatment of crosslinking was performed the same day of extraction before betaine quick freezing, and this might impact in the stability of thylakoid membranes.  Total protein was precipitated by adding ice-cold acetone in steps of 50%, 50%, 100%, 100%, and 200% of the initial solution volume, with shaking at 1000 rpm for 5 minutes between additions. Samples were stored overnight at -20°C and centrifuged at 22,000×g for 30 minutes at 4°C. The dry pellet was then resuspended in 300 µL of 0.1% sodium deoxycholate (SDC) and 100 mM tris pH 8 using mechanical assistance (2 glass beads of 4 mm in a 2 mL tube at 1000 rpm for 2 hours). Digestion was carried out overnight at 37°C using trypsin from bovine pancreas (Merck) at a 1:20 enzyme/protein ratio. Trypsin activity was stopped by heating at 90°C for 10 minutes. To dephosphorylate endogenous peptides, the digested solution was supplemented with 25 mM MgCl2, 50 mM KCl, and centrifuged at maximum speed for 5 minutes. The supernatant was separated, and the pellet was resuspended with 100 µL of 100 mM tris (pH 8). This solution underwent an additional centrifugation step to extract any remaining peptides, which were combined with the previous solution. Calf intestinal phosphatase (Quick CIP, NEB) at a concentration of 10 units/mL was added to the recovered supernatant, and it was incubated at 37°C for 8-10 hours.  Precipitation of residual SDC was induced by adjusting pH to 3 with formic acid. The solutions were then centrifuged to remove debris. Peptides were desalted using an Oasis HLB 96-well plate according to manufacturer's protocol (Waters Corporation). Cross-linked peptides were enriched using the MagReSyn® Zr-IMAC protocol (Resyn Biosciences) with minor adjustments compared to the manufacturer protocol, namely we used a beads:peptide ratio of 1:4 we increased the glycolic acid concentration to 1M in the binding buffer, and NH3 to 5% in the elution buffer. Beads were recycled by repeating the entire protocol with the same nanoparticles for each sample and then joining the final eluates, as it was shown to increase the recovery (Bortel et al. 2024). Mass Spectrometry Analysis (remember FAIMS) Phospho-enriched peptides were processed in two different NanoLC-MS/MS configurations: a Dionex UltiMate 3000 RSLCnano coupled to an Orbitrap Exploris 480 through an FAIMS Pro™ interface (CV 55-60-75) (Thermo Fisher Scientific) and a UHPLC Vanquish Neo coupled to an Orbitrap Ascend Tribid mass spectrometer (Thermo Fisher Scientific). Peptides were separated on an Aurora Ultimate C18 column (IonOpticks) using a 120-minute gradient from 2.5% to 41% acetonitrile in 0.1% formic acid at 300 nL/min. Full scan MS spectra covered 400 to 1600 m/z. MS2 ions were fragmented with normalized collision energy of 21-28-36 for the Orbitrap Exploris and 21-29-37 for the Ascend. Ions with less than 2+ charge were excluded."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For Crosslinks search data analysis was conducted using XlinkX Node in Proteome Discoverer 3.0 (Thermo Fisher Scientific) to identify cross-linked (XL) peptides with a minimum score cut-off of 40 (Klykov et al. 2018). The 20% most abundant identified proteins in the mono-link analysis (FragPipe output) were implemented as a database along with the inclusion of proteoforms with non-tryptic N-terminal cleavages. The proteoforms were obtained after including non-tryptic cleavage in FragPipe settings.  In order to conduct the study, only those cross-links that appeared in at least two out of three replicates (2 out 3) or all three replicates (3 out 3) for each condition were considered. Data filtering and formatting were conducted using an R script, which was subsequently employed to reshape the data into the input for xiNET, an online cross-link viewer developed by the Rappsilber Laboratory (Combe et al. 2015). To analyze cross-linked peptide data generated by Proteome Discoverer (PD), we developed a custom R-based pipeline for re-annotation and visualization of XL-peptides in xiNET. The analysis was performed using R version 4.2.1, incorporating packages such as tidyverse, dplyr, Biostrings, data.table, stringr, and seqinr. Input data consisted of crosslink spectrum matches (CSM) exported from PD and a reference protein sequence database. The pipeline organized data according to MS run identifiers and classified them by experimental condition. Data pre-processing included filtering out cross-links that did not meet a user-defined minimum XlinkX score threshold (for this analysis 40) and grouping them based on a minimum number of repeated cross-link hits across replicates (“2 out of 3” and “3 out of 3” replicates). Remaining data were consolidated into unique cross-links, defined by sequence and site of crosslinking, retaining the highest score, the number of spectral matches, and the cumulative precursor abundances from aggregated CSMs. Cross-links were annotated with peptide sequences, linking positions, and associated scores, and formatted for visualization in xiNET. Protein sequence re-annotation was performed by mapping peptides to a FASTA database, refining annotations originally assigned by PD This step aims to eliminate redundant proteoforms, essential for finding XLs with N-terminal residues after transient peptide cleavage. Furthermore, the pipeline generated all possible protein-pair combinations by aligning peptides to the updated database. This step is applied to distinguish between interactions that might occur between multiple proteins sharing the same peptide sequences due to high homology (e.g. light harvesting complex proteins), from protein-specific interactions."],"omics_type":["Proteomics"],"labhead":["Pascal Albanese"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Light, Photosynthesis & Metabolism (LPM) & Exploring the Dynamics of Proteomes (EDyP)  IRIG, CEA-Grenoble 17 rue des Martyrs, 38000 Grenoble, France"],"species":["Spinacia Sp.","Arabidopsis Thaliana (mouse-ear Cress)"],"publication":["Not available"],"submitter_mail":["pascal.albanese@cea.fr"],"submitter_affiliation":["Light, Photosynthesis & Metabolism (LPM) &\nExploring the Dynamics of Proteomes (EDyP) \nIRIG, CEA-Grenoble\n17 rue des Martyrs, 38000 Grenoble, France"],"submitter_country":["France"],"additional_accession":[]},"is_claimable":false,"name":"Deciphering Photosynthetic Protein Networks: A Crosslinking-MS Strategy for Studying Functional Thylakoid Membranes","description":"Photosynthesis relies on a dynamic network of protein-protein interactions that adapt to fluctuating light conditions. We present an XL-MS pipeline applied directly to functional thylakoid membranes from Arabidopsis thaliana and Spinacia oleracea. By combining PhoX crosslinker with the amphiphilic salt TMPAC, we captured reproducible structural insights into photosynthetic protein complexes while maintaining photosynthetic activity during crosslinking. The approach enables detection of hundreds of unique crosslinks within three days, expanding thylakoid protein interaction maps, and providing structural models of known and novel complexes. This study demonstrates the feasibility of probing functional photosynthetic membranes with XL-MS, paving the way for integrative analyses of dynamic organellar 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