{"code":"SASDE86","status":"Published","type_of_curve":"SEC-SAS","angular_unit":"1/nm","project":{"title":"Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.","publication":{"title":"Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.","author_list":"Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K","journal":"Nature","doi":"10.1038/s41586-019-1095-5","pmid":"30944476","published_date":"2019 Apr"},"status":"released","submitted_date":"2018-10-10","released_date":"2019-04-02"},"pddf_data":"https://www.sasbdb.org/media/p_of_R_files/SASDE86.out","intensities_data":"https://www.sasbdb.org/media/intensities_files/SASDE86.dat","intensities_log_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDE86_dat_img.png","intensities_kratky_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDE86_kratky_img.png","pddf_plot":"https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDE86_pofr_img.png","intensities_guinier_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDE86_guinier_img.png","sascif_data":"https://www.sasbdb.org/media/sascif/sascif_files/SASDE86.sascif","experiment":{"instrument":{"detector":{"type":null,"name":"Pilatus 2M","resolution":null},"name":"PETRA III","city":"DESY; Hamburg","country":"Germany","beamline_name":"EMBL P12","beam_geometry":null,"type_of_source":"X-ray synchrotron","point_source":null,"line_collimation":null,"sample_path_length":null,"line_collimation_slitlength":null,"line_collimation_integrationwidth":null,"xray_energy":null,"beam_profile_ah":null,"beam_profile_al":null},"sample":{"molecule":[{"long_name":"ATP-citrate lyase","short_name":"ACL","sequence":"AKILEGPAMKLFNKWGIPVPNYVVIMDPDRLAQLGEANKWLRESKLVVKAHEAIGGRFKL\r\n GLVKIGLNLEQAIEAAKEMLGAKVGTAEIGQVIIAEMLEHDAEFYVSIIGNKDGAELLIS\r\n KHGGVDIEDNWDSVRRIQIELDENPTIEQLTELAKDAGFEGEIAERVGKICSRLILCFDN\r\n EDAQSIEINPLVIRKSDMRFAALDAVMNVDYDARFRHADWDFKPVSEIGRPFTEAEQQIM\r\n EIDSRIKGSVKFVEVPGGEIALLTAGGGASVFYADAVVARGGTIANYAEYSGDPADWAVE\r\n ALTETICRLPNIKHIIVGGAIANFTDVKATFSGIINGFRESKSKGYLEGVKIWVRRGGPN\r\n EAQGLAAIKQLQEEGFDIHVYDRSMPMTDIVDLAMKSSILANKDTRAVIIGGVAGVNAAK\r\n RMAQFDFLVNRPLTVQAFVYPPEAGQQKEIFRGGELKNVTVYDSLAPALEEHPDINTALI\r\n YLGASRAAQAAKEALESPNIQLVSMITEGVPEKDAKRLKKLAQKLGKMLNGPSSIGIMSA\r\n GECRLGVIGGEFKNLKLCNLYRQGSFGVLTKSGGLSNEAMWLCAQNGDGITSAVAIGGDA\r\n YPGTDFVTYLEMFEKDPATKAVVMIGEVGGNLEEEAAEWLAAEPRRIKLIAAIGGTCQEV\r\n LKGAGSARSKMNALRDAGAYVPDTFGGLSKEIKKVYEELIAAGEISTEIDEAVLPELPPR\r\n VQEVMKQGEVIVEPLIRTTISDDRGEEPRYAGYAASELCSKGYGIEDVIGLLWNKKLPTR\r\n EESEIIKRIVMISADHGPAVSGAFGSILAACAGIDMPQAVSAGMTMIGPRFGGAVTNAGK\r\n YFKMAVEDYPNDIPGFLSWMKKNVGPVPGIGHRVKSVKNPDQRVKYLVSYIKNETSLHTP\r\n CLDYALEVEKVTTAKKGNLILNVDGTIGCILMDLDFPVHSLNGFFVLARTIGMIGHWIDQ\r\n NNQNSRLIRLYDYLINYAVKPEQEVPEK","organism":"Chlorobium limicola","uniprot_code":null,"uniprot_range_first":null,"uniprot_range_last":null,"oligomerization":"tetramer","molecular_type":"protein","uniprot_sequence":null,"mw":107.314,"total_mw":429.256,"number_molecules":4,"complex_state":false,"deuteration":null,"molecule_source":"biological","molecule_description":null}],"buffer":{"name":"20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, 2mM CoA","concentration_unit":null,"comment":null,"additive":null,"concentration":null,"pka":null,"ph":7.2,"deuteration":null},"purity_method":null,"name":"C. limicola ATP-citrate lyase (ACL) in HBS + Citrate + Coenzyme-A","ext_coefficient":null,"contrast":null,"specific_vol":null,"dry_vol":null,"absorbption":null,"deuteration":null,"mixture":null},"contributor":[{"affiliation":[{"short_name":"EMBL-Hamburg","address":"Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany","full_name":"European Molecular Biology Laboratory (EMBL) - Hamburg outstation","webpage":"http://www.embl-hamburg.de/index.php"}],"contributor_name":"Clement","contributor_surname":"Blanchet","orcid":null}],"concentration_method":null,"concentration_unit":null,"date":"2017-09-04","storage_temperature":20.0,"cell_temperature":20.0,"exposure_time":1.0,"number_of_frames":900,"wavelength":0.124,"sample_detector_distance":3.1,"concentration_min":null,"concentration_max":16.0,"sample_volume":null,"flow_rate":null,"s_min":0.025,"s_max":5.064,"total_exposure_time":null,"seccolumn":null},"fits":[],"estimated_volume_method":null,"pddf_software":"ATSAS GNOM","pddf_software_version":"5.0","i0_calibration_standard":null,"description":null,"experiment_description":"Synchrotron SAXS data from solutions of C. limicola acetyl citrate lyase ACL in 20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, 2mM coenzyme-A, pH 7.2 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size-exclusion chromatography SAXS (SEC-SAXS) was employed using a sample injection concentration of 16.00 mg/ml. Data were measured at through the SEC elution at 20°C. 900 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent-blank was subtracted using the CHROMIXS SEC-SAXS analysis package.","tags":[],"intensity_unit":"arbitrary","experimental_mw":420.0,"experimental_mw_error":null,"guinier_i0_mw":null,"guinier_i0_mw_error":null,"porod_mw":494.0,"porod_mw_error":null,"pddf_i0":111400.0,"pddf_i0_error":null,"guinier_i0":110407.0,"guinier_i0_error":61.0,"pddf_rg":5.8,"pddf_rg_error":null,"guinier_rg":5.69,"guinier_rg_error":0.03,"pddf_dmax":17.5,"pddf_dmax_error":null,"porod_volume":791.0,"porod_volume_error":null,"estimated_volume":null,"estimated_volume_error":null,"guinier_point_first":13,"guinier_point_last":54,"pddf_point_first":null,"pddf_point_last":null,"i0_calibration_standard_data":null,"intensities_log_log_plot":"SASDE86_datloglog_img.png","symmetry":null,"last_modified":"2023-06-21T07:56:39.492710+02:00","bragg_peak":[]}