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Crosslinked material was purified by 15-45% (v/v) glycerol gradient ultracentrifugation as above; fractions 9-11 were pooled (yielding a total of 1.0-1.2 µg protein) and assessed by SDS-PAGE (Supplementary Fig. X).  For mass spectrometry analysis, the crosslinked MCM2-7-Sld3-Sld7 sample was precipitated with acetone. The protein pellet was resolubilized in digestion buffer (8M urea in 100 mM ammonium bicarbonate) to an estimated protein concentration of 1 mg/ml. The disulfide bonds were reduced by addition of 1M Dithiothreitol (DTT) to a final concentration of 5 mM. The reaction was incubated at room temperature for 30 minutes. The free sulfhydryl groups in the sample were then alkylated by adding 500 mM iodoacetamide (final concentration of 15mM) and incubation at room temperature for 20 minutes in dark. After alkylation, additional 1M DTT was added (total concentration 10 mM) to quench excess of iodoacetamide. Next, protein samples were digested with LysC (at a 50:1 (m/m) protein to protease ratio) at 25°C for four hours. The sample was then diluted with 100 mM ammonium bicarbonate to reach a urea concentration of 1.5 M. Trypsin was added at a 50:1 (m/m) protein to protease ratio to further digest proteins overnight (~15 hours) at 25°C. Resulting peptides were desalted using C18 StageTips (Rappsilber et al., 2007). The resulting peptides were fractionated using size exclusion chromatography in order to enrich for crosslinked peptides (Leitner et al., 2013). Peptides were separated using a Superdex™ 30 Increase 3.2/300 column (GE Healthcare) at a flow rate of 10 l/minute. The mobile phase consisted of 30% (v/v) acetonitrile and 0.1% trifluoroacetic acid. The earliest six peptide-containing fractions (50 μl each) were collected. Solvent was removed using a vacuum concentrator. The fractions were then analysed by LC-MS/MS. LC-MS/MS analysis was performed using an Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific), connected to an Ultimate 3000 RSLCnano system (Dionex, Thermo Fisher Scientific). Each size exclusion chromatography (SEC) fraction was resuspended in 1.6% v/v acetonitrile 0.1% v/v formic acid and analysed with LC-MS/MS acquisitions. For four of total six SEC fractions that has adequate material, an duplicated LC-MS/MS acquisition were carried out. Peptides were injected onto a 50-centimetre EASY-Spray C18 LC column (Thermo Scientific) that is operated at 50 °C column temperature. Mobile phase A consists of water, 0.1% v/v formic acid and mobile phase B consists of 80% v/v acetonitrile and 0.1% v/v formic acid. Peptides were loaded and separated at a flowrate of 0.3 μl/min. Peptides were separated by applying a gradient ranging from 2% to 55% B over 102.5 minutes. The slope of the gradients were optimized for each SEC fraction. Following the separating gradient, the content of B was ramped to 55% and 95% within 2.5 minutes each. Eluted peptides were ionized by an EASY-Spray source (Thermo Scientific) and introduced directly into the mass spectrometer. The MS data is acquired in the data-dependent mode with the top-speed option. For each 2.5-second acquisition cycle, the full scan mass spectrum was recorded in the Orbitrap with a resolution of 120,000. The ions with a charge state from 3+ to 7+ were isolated and fragmented using higher-energy collisional dissociation (HCD). For each isolated precursor, stepped collision energy (26%, 28% and 30%) was applied. The fragmentation spectra were then recorded in the Orbitrap with a resolution of 60,000. Dynamic exclusion was enabled with single repeat count and 60 second exclusion duration."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["MS2 peak lists were generated from the raw mass spectrometric data files using the MSConvert module in ProteoWizard (version 3.0.11729). Precursor and fragment m/z values were recalibrated. Identification of crosslinked peptides was carried out using xiSEARCH software (https://www.rappsilberlab.org/software/xisearch) (version 1.7.6.4) (PMID 31556486). The peak lists were searched against the sequences and the reversed sequences of 5 pombe condensin subunits. The following parameters were applied for the search: MS accuracy, 3 ppm; MS2 accuracy, 5 ppm; enzyme, trypsin (with full tryptic specificity); allowed number of missed cleavages, 3; missing monoisotopic peak, 2;cross-linker, BS3 (the reaction specificity was assumed to be for lysine, serine, threonine, tyrosine and protein N termini); fixed modifications, carbamidomethylation on cysteine; variable modifications,  oxidation on methionine, hydrolyzed BS3, Tris reacted BS3, acetylation on lysine and deamidation on asparagine; maximum variable modification per peptide, 2. Identified crosslinked peptide candidates that has at least three matched fragment ions in each crosslinked peptide and at least two fragments containing residues of both peptides were filtered using xiFDR (ref. PMID: 29256016). A false discovery rate of 1% on residue-pair level was applied with “boost between” option selected."],"omics_type":["Proteomics"],"labhead":["Juri Rappsilber"],"instrument_platform":[""],"labhead_affiliation":["TU Berlin"],"submission_type":["COMPLETE"],"species":["Saccharomyces Cerevisiae (baker's Yeast)"],"submitter_mail":["zhuo.chen@tu-berlin.de"],"publication":["Not available"],"submitter_affiliation":["Technischen Universität Berlin"],"submitter_country":["Germany"],"doi":["10.6019/PXD070193"],"additional_accession":[]},"is_claimable":false,"name":"Crosslinking MS analysis of MCM2-7 DH-Sld3/7 complex","description":"interrogate the 3D organization of the MCM2-7 DH-Sld3/7 complex espetically the flexible Sld3/7 regions, the MCM2-7 DH-Sld3/7 complex was analyzed by crosslinking 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