{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90B_human_2025.08.03.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90B_human_2025.08.03.filtered_cross-linked_spectra.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90-BDG_MS2_310K_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90-BDG_MS2_310K_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90-BDG_MS2_310K_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90-BDG_MS2_323K_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90-BDG_MS2_298K_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90-BDG_MS2_323K_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90-BDG_MS2_298K_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90-BDG_MS2_323K_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90-BDG_MS2_298K_R1.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066889/HSP90B_human.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["tang_chun@pku.edu.cn"],"submitter":["yida jiang"],"technology_type":["Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"software":["Not available"],"submitter_keywords":["Cleavable cross-linkers","Photo-cross-linking","Hsp90β","Diazirine","Machine learning (decision tree)"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD066889"],"sample_protocol":["Synthesis of BDG Disuccinimidyl glutarate (393 mg, 1.2 mmol, Aikonchem, CAS Number 79642-50-5) was dissolved in 10 mL dichloromethane. (3-methyl-3H-diazirin-3-yl)methanamine hydrochloride (271 mg, 2 mmol, DreamChem, CAS number 882516-45-2) was added while stirring. The mixture was neutralized with slow addition of triethylamine (665 μL, 4.8 mmol) and stirred in the dark at room temperature for 24 hours. The reaction mixture was successively washed with saturated ammonium chloride solution (3 × 7.5 mL) and saturated sodium bicarbonate solution (3 × 7.5 mL). The combined aqueous phases were extracted with dichloromethane (3 × 10 mL); the organic phases were combined and dried over anhydrous sodium sulfate (10 g) for 24 hours, and concentrated under reduced vapor pressure to afford an off-white solid crude product (201 mg). The crude product was slurred with methyl tert-butyl ether (10 mL) in the dark for 1 hour, filtered through a SYNTHWARE® F-type filter funnel (Synthware, F363019F), and washed with methyl tert-butyl ether (3 × 10 mL). Upon vacuum drying, 137.7 mg of white powder product, N1,N5-bis((3-methyl-3H-diazirin-3-yl)methyl)glutaramide, abbreviated as BDG, was obtained with a 52% yield. Photo-cross-linking reaction The protein was dissolved in SEC buffer (20 mM HEPES, 20 mM NaCl, 5 mM MgCl2, pH 7.8) to a final concentration of 1 µg/uL, and were aliquoted into 20 μL. The sample was incubated in the dark after the addition of 10 μL 10 mM cross-linker. For SDA and BDG, photo-cross-linking reactions were performed with optical power density [hv] = 25 mW/cm2 and irradiation time of 2 min. Immediately after irradiation, each sample was added with 1 mL pre-chilled acetone and placed at −20 °C overnight to fully precipitate the protein, which was then collected by centrifugation at 15,000 rpm for an hour. Trypsin digestion The protein was solubilized in 8 M urea in 1× PBS. To reduce disulfide bonds and carbamidomethylate cysteine residues, a 1:10 volume (30 µL) of reduction/alkylation buffer (containing 100 mM TCEP and 400 mM 2-chloroacetamide, adjusted to pH 7–8 with KOH) was added to the sample. The mixture was incubated for 1 hour at 25 °C in the dark. Following reduction and alkylation, the sample was diluted to a final urea concentration of less than 2 M using 1× PBS. Trypsin digestion was carried out by adding trypsin (Promega) at an enzyme-to-substrate ratio of 1:30, and the reaction was allowed to proceed overnight at 37 °C. The digested peptides were acidified with the addition of neat trifluoroacetic acid (TFA) to a final concentration of 1%, and the sample was centrifuged to rid of any precipitates. Peptides were then desalted using tC18 RP solid-phase extraction cartridges (Waters). The cartridges were pre-equilibrated with wash solvent (0.1% TFA), and peptides were eluted with 0.1% TFA in 50% acetonitrile (ACN). Eluted peptides were dried by vacuum centrifugation prior to mass spectrometry analysis. LC-MSn analysis The digestion products were separated using a 120-minute gradient elution at a flow rate of 0.300 µL/min on a Thermo Dionex Ultimate 3000 HPLC system, which was coupled to a Thermo Scientific Orbitrap Fusion mass spectrometer. The analytical separation was performed on a homemade fused-silica capillary column (100 µm inner diameter × 150 mm length; Upchurch, Oak Harbor, WA) packed with C18 resin (1.9 µm particle size, 120 Å pore size; Dr. Maisch, Germany). Mobile phase A consisted of 0.1% formic acid in water, and mobile phase B contained 80% acetonitrile and 0.1% formic acid. Mass spectrometric analysis was carried out in data-dependent acquisition (DDA) mode using Xcalibur 4.1 software. A high-resolution full-scan MS spectrum (m/z 350–1550) was acquired in the Orbitrap at a resolution of 120,000. This was followed by top-speed MS/MS (MS2) scans, also performed in the Orbitrap, for the fragmentation and detection of the most abundant precursor ions."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Cross-linked peptides were analyzed using the pLink (version 3.0.16) with integrated scoring and search capabilities. The following parameters were applied for all searches: a mass tolerance of ±20 ppm for both MS1 and MS2 spectra, trypsin as the digestion enzyme with full specificity and allowing up to three missed cleavages, and a false discovery rate (FDR) threshold of 5%. Carbamidomethylation of cysteine was set as a fixed modification, and oxidation of methionine and N-terminal acetylation as variable modifications. For cross-linking analysis, different parameters were set depending on the type of cross-linker used. For SDA and photo-Leu cross-links, Site 1 was restricted to lysine (K) for SDA or leucine (L) for photo-Leu, while Site 2 was restricted to polar residues (D, E, S, T, Y, H). The linker mass and fragment masses were defined as follows: for SDA, linker mass = 82.042, long mass (sz) = 82.042, and short mass (sc) = 0.000; for photo-Leu, linker mass = –16.031, long mass (sz) = –16.031, and short mass (sc) = 0.000. For BDG cross-links, both Site 1 and Site 2 were restricted to polar residues (D, E, S, T, Y, H), with a linker mass of 210.137, long mass (sz) = 210.137, and short mass (sc) = 0.000. Additional long and short mass combinations (170.106 and 40.031) were also considered to account for alternative fragmentation. For BS3 cross-links, both cross-linking sites were restricted to lysine (K). To estimate the decoy/contamination rate, export all the search results that include decoys in the search configure. After the database search, insert the relevant paths into the script available at https://github.com/Tanglab-PKU/sFFP_tools. Adjust the parameters according to the type of cross-linker used. Run the script sequentially. First, use either the ML model or the simplified model to filter out potential negative data. Then, perform sorting based on the score for quality control. The scripts for xiSEARCH and MeroX can be used in the same way as pLink."],"omics_type":["Proteomics"],"labhead":["Chun Tang"],"instrument_platform":[""],"labhead_affiliation":["Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["jiangyida@pku.edu.cn"],"publication":["Not available"],"submitter_affiliation":["Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"pLink Characterizing the dynamic oligomerization of HSP90β using photo-cross-linking","description":"Cross-linking mass spectrometry (XL-MS) is a transformative tool for probing protein structures. While conventional chemical crosslinkers exhibit well-defined chemistry for specific residues, photo-crosslinkers, despite their superior reactivity, have been hindered by incomplete mechanistic understanding and a lack of analytical frameworks. Here, we demonstrate that diazirine-based photo-crosslinks are inherently MS-cleavable—a novel property but also complicates spectral interpretation for overlapping peptide backbone and crosslinker side-chain fragments. Leveraging diagnostic side-chain fragmentation fingerprints, we developed a machine learning model that significantly improves ion coverage and reduces false discovery rates when combined with existing search algorithms. Further, we designed a homo-bifunctional diazirine crosslinker that allows for true on-demand photo-crosslinking. Empowered, we captured transient tetrameric assemblies of human HSP90β and revealed structural transitions in association equilibrium upon heat stress—features inaccessible with conventional chemical crosslinking. Together, our work establishes a new paradigm of XL-MS, combining the temporal sensitivity and precision of photo-activation with analytical 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