{"id":11452,"date":"2024-10-09T18:39:49","date_gmt":"2024-10-09T09:39:49","guid":{"rendered":"https:\/\/www.protein.osaka-u.ac.jp\/?page_id=11452"},"modified":"2025-10-14T16:52:49","modified_gmt":"2025-10-14T07:52:49","slug":"facilities","status":"publish","type":"page","link":"http:\/\/www2.protein.osaka-u.ac.jp\/en\/joint\/facilities\/","title":{"rendered":"TOP-END FACILITIES"},"content":{"rendered":"<div id=\"container\" class=\"joint joint_facilities --en\">\r\n  <div class=\"joint_sub_inner\">\r\n    <div class=\"joint_sub_column\">\r\n      <div class=\"joint_sub_fv --facilities\">\r\n      <ul class=\"all_pankuzu\">\r\n          <li>\r\n            <a href=\"http:\/\/www2.protein.osaka-u.ac.jp\/\"><img decoding=\"async\" src=\"http:\/\/www2.protein.osaka-u.ac.jp\/wp-content\/themes\/ipr\/images\/all_img_home.png\" altSPring=\"\" width=\"15\"><\/a>\r\n          <\/li>\r\n          <li>\r\n          <a href=\"http:\/\/www2.protein.osaka-u.ac.jp\/joint\/\" class=\"_back\">JOINT USAGE \/ RESEARCH CENTER<\/a>\r\n          <\/li>\r\n          <li>\r\n            <span class=\"_current\">TOP-END FACILITIES<\/span>\r\n          <\/li>\r\n        <\/ul>\r\n        <div class=\"all_title\">\r\n          <h1 class=\"all_title_big\">\r\n            TOP-END FACILITIES\r\n          <\/h1>\r\n        <\/div>\r\n      <\/div>\r\n      <section>\r\n        <!-- \u3053\u3053\u304b\u3089\u30b3\u30f3\u30c6\u30f3\u30c4 \/ facility -->\r\n        <div class=\"all_column_big content_max\" id=\"facility\">\r\n          <div class=\"all_column_big_title\">\r\n            <div class=\"all_vertical_border_title\">\r\n              <h2 class=\"all_vertical_border_title_big\">TOP-END FACILITIES<\/h2>\r\n            <\/div>\r\n          <\/div>\r\n          <div class=\"all_column_big_img\">\r\n            <p>\r\n              <img decoding=\"async\" src=\"http:\/\/www2.protein.osaka-u.ac.jp\/wp-content\/themes\/ipr\/images\/joint_img_column_big_facility.jpg\" alt=\"\">\r\n              <span class=\"pic_copy\">\u24b8RIKEN<\/span>\r\n            <\/p>\r\n          <\/div>\r\n          <div class=\"all_column_big_box all_text facilities_column_big_box_en\">\r\n            <p>\r\n              IPR operates state-of-the-art facilities for modern structural biology research, including X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cryo-electron microscopy (cryo-EM).\r\n            <\/p>\r\n            <p>\r\n              As for X-ray crystallography, we operate a contract beamline (BL44XU) for macromolecular assemblies at the SPring-8 synchrotron facility, which is approximately 120 km west of IPR in Nishi-Harima, Hyogo. The institute houses and operates up to nine NMR spectrometers, including the flagship solution NMR model (950 MHz) and solid-state NMR with an ultra-highly sensitive DNP system, operating 24\/7. \r\n            <\/p>\r\n            <p>\r\n              IPR also manages three cryo-EM scopes including Titan Krios (Thermo Fisher Scientific), Talos Arctica (Thermo Fisher Scientific), and JEM-2200FS (JEOL), all equipped with direct electron detectors capable of world-class high-resolution single-particle analysis and electron tomography. \r\n            <\/p>\r\n          <\/div>\r\n        <\/div>\r\n        <div class=\"joint_facility joint_facility_en\">\r\n          <div class=\"content\">\r\n            <div class=\"joint_facility_sec\">\r\n              <p class=\"all_ham_title\">\r\n                <a href=\"\"><span>Beamline for Biological Macromolecular Assemblies at SPring-8 (BL44XU)<\/span><\/a>\r\n              <\/p>\r\n              <div class=\"joint_facility_content\">\r\n                <div class=\"joint_facility_content_top\">\r\n                  <p class=\"joint_facility_content_img\">\r\n                    <img decoding=\"async\" src=\"http:\/\/www2.protein.osaka-u.ac.jp\/wp-content\/themes\/ipr\/images\/joint_img_facility_spring.jpg\" alt=\"\">\r\n                  <\/p>\r\n                  <div class=\"joint_facility_content_text\">\r\n                    <p class=\"all_text\">\r\n                      The beamline for X-ray crystallography of biological macromolecules at SPring-8 (BL44XU) is available to researchers who belong to academic organizations throughout the world. Regular applications involving non-proprietary proposals are received once per year, and urgent applications can be accepted all year around. More than 50% of the total beamtime is used for collaborative research programs of the Institute for Protein Research. This beamline is specially designed for data collection of large unit cell crystals for analyzing biological macromolecular assemblies, such as protein complexes, protein-nucleic acid complexes, and viruses.\r\n                    <\/p>\r\n                    <table class=\"all_border_table\">\r\n                      <tr>\r\n                        <th>\r\n                          <p>Year established<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>1999 (Upgraded in 2001, 2003, 2006, 2009, 2011, 2012, 2015, 2018)<\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                      <tr>\r\n                        <th>\r\n                          <p>Facility specification<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>\r\n                            <span>\r\n                              Light source:<br>\r\n                              <span>Undulator<\/span>\r\n                            <\/span>\r\n                            <span>\r\n                              Optics:<br>\r\n                              <span>N2-cooled double crystal monochromator, Horizontal and vertical focusing mirrors<\/span>\r\n                            <\/span>\r\n                            <span>\r\n                              Detector:<br>\r\n                              <span>Pixel array detector (Eiger X 16M)<\/span>\r\n                            <\/span>\r\n                          <\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                    <\/table>\r\n                  <\/div>\r\n                <\/div>\r\n              <\/div>\r\n            <\/div>\r\n            <div class=\"joint_facility_sec\">\r\n              <p class=\"all_ham_title\">\r\n                <a href=\"\"><span>Solution NMR Spectrometer in an Ultra-high Magnetic Field<\/span><\/a>\r\n              <\/p>\r\n              <div class=\"joint_facility_content\">\r\n                <div class=\"joint_facility_content_top\">\r\n                  <p class=\"joint_facility_content_img\">\r\n                    <img decoding=\"async\" src=\"http:\/\/www2.protein.osaka-u.ac.jp\/wp-content\/uploads\/2022\/10\/nmr-.png\" alt=\"\">\r\n                  <\/p>\r\n                  <div class=\"joint_facility_content_text\">\r\n                    <p class=\"all_text\">\r\n                      The ultra high field NMR instruments ( \u00b9H resonance frequency of 950 and 800 MHz) enable the analysis of 3D structures dynamics and interactions of high molecular-weight protein complexes and organic molecules at low concentrations, which markedly exceeds the performance of conventional spectrometers. This device provides one of the world\u2019s highest magnetic fields, following a 1200 MHz spectrometer.<br>\r\n                      600, 500, and 400 MHz NMR instruments are also available, allowing structure, dynamics, and interaction analysis of proteins and small molecules to be conducted.\r\n                    <\/p>\r\n                    <table class=\"all_border_table\">\r\n                      <tr>\r\n                        <th>\r\n                          <p>Year established<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>2010 (Upgraded in 2013, 2014 and 2020)<\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                      <tr>\r\n                        <th>\r\n                          <p>Equipments<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>\r\n                            <span>\r\n                              950, 800, 600, 500, and 400 MHz NMR Spectroscopy (BRUKER) *<br>\r\n                              <span style=\"font-size: 14px;\">* TopSpin 3.6.2; Remote measurement is supported (2020 upgraded).<\/span>\r\n                            <\/span>\r\n                            <span>\r\n                              Spectrometer\uff1a<br>\r\n                              <span>\r\n                              Avance III 950<br>\r\n                              Avance III HD 800, 600, 400 (2013 upgraded)  Avance III HD 500 (2014 upgraded)\r\n                              <\/span>\r\n                            <\/span>\r\n                            <span>\r\n                              Probe\uff1a<br>\r\n                              <span style=\"line-height: 1.2;\">\r\n                                CRYO TCI probe\uff3b950MHz\uff3d<br>\r\n                                CRYO TXI probe\uff3b800MHz\uff3d<br>\r\n                                CRYO QCI-P probe [600MHz]<br>\r\n                                CRYO BBO H\/F probe [500 MHz]<br>\r\n                                BBFO, TXI probe [400MHz]<br>\r\n                              <\/span>\r\n                            <\/span>\r\n                            <span>\r\n                              Sample changer:<br>\r\n                              <span>\r\n                                SampleCaseCooled [600MHz] (2020 upgraded) SampleXpress [400MHz]\r\n                              <\/span>\r\n                            <\/span>\r\n                          <\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                    <\/table>\r\n                  <\/div>\r\n                <\/div>\r\n              <\/div>\r\n            <\/div>\r\n            <div class=\"joint_facility_sec\">\r\n              <p class=\"all_ham_title\">\r\n                <a href=\"\"><span>Ultra-High-Sensitivity Solid-State NMR Spectrometers<\/span><\/a>\r\n              <\/p>\r\n              <div class=\"joint_facility_content\">\r\n                <div class=\"joint_facility_content_top\">\r\n                  <p class=\"joint_facility_content_img\">\r\n                    <img decoding=\"async\" src=\"http:\/\/www2.protein.osaka-u.ac.jp\/wp-content\/themes\/ipr\/images\/joint_img_facility_nmr2.jpg\" alt=\"\">\r\n                  <\/p>\r\n                  <div class=\"joint_facility_content_text\">\r\n                    <p class=\"all_text\">\r\n                      These spectrometers enable the analysis of the structures and functions of biomolecules in non-crystalline solid states, such as proteins in lipid bilayers and amyloid proteins. The two DNP-NMR spectrometers are equipped with gyrotrons generating high-power submillimeter waves and sample-rotation systems at cryogenic temperatures. Thereby, they generate hyper-polarization that provide the world\u2019s highest performance in NMR sensitivity.\r\n                    <\/p>\r\n                    <table class=\"all_border_table\">\r\n                      <tr>\r\n                        <th>\r\n                          <p>Year established<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>2001 (Upgraded in 2006 and 2013)<\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                      <tr>\r\n                        <th>\r\n                          <p>Equipment<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>\r\n                            500 MHz Solid-State NMR Spectrometer<br>\r\n                            700 MHz Solid-State NMR Spectrometer<br>\r\n                            400MHz\/263GHz Solid-State DNP-NMR Spectrometer<br>\r\n                            600MHz\/396GHz Solid-State DNP-NMR Spectrometer<br>\r\n                            700MHz\/461GHz Solid-State DNP-NMR Spectrometer\r\n                          <\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                    <\/table>\r\n                  <\/div>\r\n                <\/div>\r\n              <\/div>\r\n            <\/div>\r\n            <div class=\"joint_facility_sec\">\r\n              <p class=\"all_ham_title\">\r\n                <a href=\"\"><span>Cryo-electron Microscopes<\/span><\/a>\r\n              <\/p>\r\n              <div class=\"joint_facility_content\">\r\n                <div class=\"joint_facility_content_top\">\r\n                  <p class=\"joint_facility_content_img\">\r\n                    <img decoding=\"async\" src=\"http:\/\/www2.protein.osaka-u.ac.jp\/wp-content\/themes\/ipr\/images\/joint_img_facility_cryo.jpg\" alt=\"\">\r\n                  <\/p>\r\n                  <div class=\"joint_facility_content_text\">\r\n                    <p class=\"all_text\">\r\n                      IPR is equipped with cutting-edge cryo-electron microscopy instruments for the precise structural analysis of biological samples. In addition to the single-particle analysis for purified biomolecules, we cover all aspects of electron structural studies, including electron tomography for biomolecules in cells as well as microED for small molecules. IPR offers a complete range of equipment for sample preparation, such as a high-pressure freezing, a cryo-microtome, and a blot-free cryo-grid preparation robot, to meet diverse observation needs.\r\n                    <\/p>\r\n                    <table class=\"all_border_table\">\r\n                      <tr>\r\n                        <th>\r\n                          <p>Year extablished<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>2012 (Upgraded in 2015 and 2017)<\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                      <tr>\r\n                        <th>\r\n                          <p>Equipments<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>\r\n                            120kV H-7650\uff082010-\uff09<br>\r\n                            200kV JEM-2200FS\uff082012-\uff09<br>\r\n                            300kV Titan Krios G2\uff082015-\uff09<br>\r\n                            200kV Talos Arctica\uff082017-\uff09\r\n                          <\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                    <\/table>\r\n                  <\/div>\r\n                <\/div>\r\n              <\/div>\r\n            <\/div>\r\n            <!-- <div class=\"joint_facility_sec\">\r\n              <p class=\"all_ham_title\">\r\n                <a href=\"\"><span>High-performance X-ray Diffractometer<\/span><\/a>\r\n              <\/p>\r\n              <div class=\"joint_facility_content\">\r\n                <div class=\"joint_facility_content_top\">\r\n                  <p class=\"joint_facility_content_img\">\r\n                    <img decoding=\"async\" src=\"[wp_theme_uri]\/images\/joint_img_facility_x.jpg\" alt=\"\">\r\n                  <\/p>\r\n                  <div class=\"joint_facility_content_text\">\r\n                    <p class=\"all_text\">\r\n                      Three X-ray diffractometers with cryo-stream coolers for protein crystallography are mounted on two rotating anode X-ray generators.\r\n                    <\/p>\r\n                    <table class=\"all_border_table\">\r\n                      <tr>\r\n                        <th>\r\n                          <p>Year established<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>2003 (Upgraded in 2011 and 2016)<\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                      <tr>\r\n                        <th>\r\n                          <p>Equipments<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>\r\n                            <span>\r\n                              X-ray generator\uff1a<br>\r\n                              <span>RIGAKU FR-E SuperBright&#8482;, Confocal VariMax Mirror<\/span>\r\n                            <\/span>\r\n                            <span>\r\n                              Detector\uff1a<br>\r\n                              <span>RIGAKU XtaLAB SynergyCustom<\/span>\r\n                            <\/span>\r\n                          <\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                    <\/table>\r\n                  <\/div>\r\n                <\/div>\r\n              <\/div>\r\n            <\/div> -->\r\n            <div class=\"joint_facility_sec\">\r\n              <p class=\"all_ham_title\">\r\n                <a href=\"\"><span>Protein sequencer (Shimadzu PPSQ-53A)<\/span><\/a>\r\n              <\/p>\r\n              <div class=\"joint_facility_content\">\r\n                <div class=\"joint_facility_content_top\">\r\n                  <p class=\"joint_facility_content_img\">\r\n                    <img decoding=\"async\" src=\"http:\/\/www2.protein.osaka-u.ac.jp\/wp-content\/themes\/ipr\/images\/joint_img_facility_protein.jpg\" alt=\"\">\r\n                  <\/p>\r\n                  <div class=\"joint_facility_content_text\">\r\n                    <div class=\"all_text\">\r\n                      <p>\r\n                        Amino acid sequence (primary structure) of a protein is an essential information for studying protein structure and function. Full-length amino acid sequences of proteins are easily obtained from the information of genome, however, proteins in the actual living system are sometimes truncated at N-terminus or\/and C-terminus or modified by post-translational modification.\r\n                      <\/p>\r\n                      <p>\r\n                        Therefore, chemical sequencing using Edman degradation method gives valuable sequence information. In addition, the amino acid sequences of proteins of a species without genome information must be directly analyzed with the protein samples themselves.\r\n                      <\/p>\r\n                      <p>\r\n                        Our protein sequencer, Shimadzu PPSQ-53A can analyze the N-terminal sequence of a protein or a peptide. We accept requests from outside IPR as commissioned analyses.\r\n                      <\/p>\r\n                    <\/div>\r\n                    <table class=\"all_border_table\">\r\n                      <tr>\r\n                        <th>\r\n                          <p>Year established<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>2019<\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                      <tr>\r\n                        <th>\r\n                          <p>Equipment<\/p>\r\n                        <\/th>\r\n                        <td>\r\n                          <p>Shimadzu PPSQ-53A<\/p>\r\n                        <\/td>\r\n                      <\/tr>\r\n                    <\/table>\r\n                  <\/div>\r\n                <\/div>\r\n              <\/div>\r\n            <\/div>\r\n          <\/div>\r\n        <\/div>\r\n      <\/section>\r\n    <\/div>\r\n    \n  <div class=\"joint_side_column --en\">\n      <div class=\"side_inner\">\n          <p class=\"joint_side_title\">\n              <span class=\"c-en\">Navigation Menu<\/span>\n          <\/p>\n          <ul class=\"joint_side_nav\">\n              <li class=\"_back\">\n                  <a href=\"http:\/\/www2.protein.osaka-u.ac.jp\/en\/joint\/\">\n                    <span class=\"_line\">Return to Index<\/span>\n                  <\/a>\n              <\/li>\n              <li>\n                  <a href=\"http:\/\/www2.protein.osaka-u.ac.jp\/joint\/information\/\">\n                      <span class=\"_line\">APPLICATION<br class=\"\">GUIDELINES<\/span>\n                  <\/a>\n              <\/li>\n              <li>\n                  <a href=\"http:\/\/www2.protein.osaka-u.ac.jp\/joint\/overview\/\">\n                      <span class=\"_line\">ABOUT US<\/span>\n                  <\/a>\n              <\/li>\n              <li>\n                  <a href=\"http:\/\/www2.protein.osaka-u.ac.jp\/joint\/database\/\">\n                      <span class=\"_line\">DATABASE<\/span>\n                  <\/a>\n              <\/li>\n              <li>\n                  <a href=\"http:\/\/www2.protein.osaka-u.ac.jp\/joint\/facilities\/\">\n                      <span class=\"_line\">TOP-END<br class=\"_change\">FACILITIES<\/span>\n                  <\/a>\n              <\/li>\n              <li class=\"enquiry_list\">\n                  <div class=\"_inner\">\n                      <p>\n                        CONTACT US\n                      <\/p>\n                      <span class=\"nsm_03\">tanpakuken-kyoten,office.osaka-u.ac.jp<\/span>\n                      <span class=\"nsm_04\">p-con,protein.osaka-u.ac.jp<\/span>\n                  <\/div>\n              <\/li>\n          <\/ul>\n      <\/div>\n  <\/div>\r\n  <\/div>\r\n  \n  <div class=\"contact_under\">\n    <div class=\"joint_outcome_contact\">\n      <div class=\"all_joint_contact_top\">\n        <p class=\"all_joint_contact_title\">CONTACT<\/p>\n        <!--<p class=\"all_text\">\n          \u5171\u540c\u5229\u7528\u30fb\u5171\u540c\u62e0\u70b9\u306b\u95a2\u3059\u308b<span class=\"all_new_line\">\u304a\u554f\u3044\u5408\u308f\u305b\u306f\u4e0b\u8a18\u307e\u3067<\/span>\n        <\/p>-->\n      <\/div>\n      <div class=\"all_joint_contact_bottom\">\n        <ul class=\"all_joint_contact_bottom_list\">\n          <li class=\"all_joint_contact_bottom_mail\">\n            <a href=\"mailto:tanpakuken-kyoten@office.osaka-u.ac.jp\" class=\"all_bold\"><span>make an inquiry<\/span><\/a>\n          <\/li>\n        <\/ul>\n        <p class=\"all_text\">\n          Project Team of Joint Usage \/ Research Center,<br>\n          <span class=\"all_new_line\">Institute for Protein Research, The University of Osaka\n          3-2 Yamadaoka, Suita, <\/span>Osaka 565-0871, JAPAN\n          <li>&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp; E-mail: tanpakuken-kyoten[at]office.osaka-u.ac.jp (change [at] to @)<\/li>\n        <\/p>\n      <\/div>\n    <\/div>\n  <\/div>\r\n<\/div>","protected":false},"excerpt":{"rendered":"<p>JOINT USAGE \/ RESEARCH CENTER TOP-END FACILITIES TOP-END FACILITIES TOP-END FACILITIES \u24b8RIKEN IPR operates state-of-the-art facilities for modern structural biology research, including X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cryo-electron microscopy (cryo-EM). As for X-ray crystallography, we operate a contract beamline (BL44XU) for macromolecular assemblies at the SPring-8 synchrotron facility, which is approximately 120 [&hellip;]<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":80,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_locale":"en_US","_original_post":"http:\/\/e820.xsrv.jp\/protein-wp\/?page_id=50","footnotes":""},"class_list":["post-11452","page","type-page","status-publish","hentry","en-US"],"aioseo_notices":[],"_links":{"self":[{"href":"http:\/\/www2.protein.osaka-u.ac.jp\/wp-json\/wp\/v2\/pages\/11452","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/www2.protein.osaka-u.ac.jp\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"http:\/\/www2.protein.osaka-u.ac.jp\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"http:\/\/www2.protein.osaka-u.ac.jp\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"http:\/\/www2.protein.osaka-u.ac.jp\/wp-json\/wp\/v2\/comments?post=11452"}],"version-history":[{"count":4,"href":"http:\/\/www2.protein.osaka-u.ac.jp\/wp-json\/wp\/v2\/pages\/11452\/revisions"}],"predecessor-version":[{"id":13993,"href":"http:\/\/www2.protein.osaka-u.ac.jp\/wp-json\/wp\/v2\/pages\/11452\/revisions\/13993"}],"up":[{"embeddable":true,"href":"http:\/\/www2.protein.osaka-u.ac.jp\/wp-json\/wp\/v2\/pages\/80"}],"wp:attachment":[{"href":"http:\/\/www2.protein.osaka-u.ac.jp\/wp-json\/wp\/v2\/media?parent=11452"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}