<emd xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" emdb_id="EMD-1005" version="3.0.1.1" xsi:schemaLocation="https://github.com/emdb-empiar/emdb-schemas/blob/master/v3/v3_0_1_1/emdb_relaxed.xsd">
   <admin>
      <current_status>
         <code>REL</code>
         <processing_site>PDBe</processing_site>
      </current_status>
      <sites>
         <deposition>PDBe</deposition>
         <last_processing>PDBe</last_processing>
      </sites>
      <key_dates>
         <deposition>2002-08-28</deposition>
         <header_release>2002-08-30</header_release>
         <map_release>2003-08-30</map_release>
         <update>2014-10-22</update>
      </key_dates>
      <title>Structure of the Escherichia coli ribosomal termination complex with release factor 2.</title>
      <authors_list>
         <author>Klaholz BP</author>
         <author>Pape T</author>
         <author>Zavialov AV</author>
         <author>Myasnikov AG</author>
         <author>Orlova EV</author>
         <author>Vestergaard B</author>
         <author>Ehrenberg M</author>
         <author>van Heel M</author>
      </authors_list>
      <keywords>
         </keywords>
   </admin>
   <crossreferences>
      <citation_list>
         <primary_citation>
            <journal_citation published="true">
               <author order="1">Klaholz BP</author>
               <author order="2">Pape T</author>
               <author order="3">Zavialov AV</author>
               <author order="4">Myasnikov AG</author>
               <author order="5">Orlova EV</author>
               <author order="6">Vestergaard B</author>
               <author order="7">Ehrenberg M</author>
               <author order="8">van Heel M</author>
               <title>Structure of the Escherichia coli ribosomal termination complex with release factor 2.</title>
               <journal>NATURE</journal>
               <volume>421</volume>
               <first_page>90</first_page>
               <last_page>94</last_page>
               <year>2003</year>
               <external_references type="PUBMED">12511961</external_references>
               <external_references type="DOI">doi:10.1038/nature01225</external_references>
            </journal_citation>
         </primary_citation>
      </citation_list>
      <pdb_list>
         <pdb_reference>
            <pdb_id>1ml5</pdb_id>
            <relationship>
               <in_frame>FULLOVERLAP</in_frame>
            </relationship>
         </pdb_reference>
      </pdb_list>
   </crossreferences>
   <sample>
      <name>release factor RF2 bound to E. coli ribosomes</name>
      <supramolecule_list>
         <sample_supramolecule supramolecule_id="1000">
            <name>release factor RF2 bound to E. coli ribosomes</name>
            <oligomeric_state>monomer</oligomeric_state>
            <number_unique_components>2</number_unique_components>
            <molecular_weight>
               <experimental units="MDa">2.3</experimental>
               <method>sedimentation</method>
            </molecular_weight>
         </sample_supramolecule>
         <complex_supramolecule supramolecule_id="1">
            <name synonym="ribosome">ribosome</name>
            <details>Proteins L7/L12 of the LSU 50S subunit are not seen
 in the map</details>
            <recombinant_exp_flag>false</recombinant_exp_flag>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
            </natural_source>
            <recombinant_expression database="NCBI">
               </recombinant_expression>
            <molecular_weight>
               <experimental units="MDa">2.3</experimental>
               <theoretical units="MDa">2.3</theoretical>
            </molecular_weight>
            <ribosome-details>ribosome-prokaryote: LSU 50S</ribosome-details>
         </complex_supramolecule>
      </supramolecule_list>
      <macromolecule_list>
         <protein_or_peptide macromolecule_id="1">
            <name synonym="RF2">release factor 2</name>
            <natural_source database="NCBI">
               <organism ncbi="469008">Escherichia coli BL21(DE3)</organism>
               <strain>BL21 (DE3)</strain>
            </natural_source>
            <molecular_weight>
               <experimental units="MDa">0.040</experimental>
               <theoretical units="MDa">0.04</theoretical>
            </molecular_weight>
            <number_of_copies>1</number_of_copies>
            <oligomeric_state>monomer</oligomeric_state>
            <recombinant_exp_flag>true</recombinant_exp_flag>
            <recombinant_expression database="NCBI">
               <recombinant_organism ncbi="562">Escherichia coli</recombinant_organism>
               <recombinant_plasmid>pET11a</recombinant_plasmid>
            </recombinant_expression>
            <sequence>
               <external_references type="INTERPRO">IPR004374</external_references>
            </sequence>
         </protein_or_peptide>
      </macromolecule_list>
   </sample>
   <structure_determination_list>
      <structure_determination structure_determination_id="1">
         <method>singleParticle</method>
         <aggregation_state>particle</aggregation_state>
         <specimen_preparation_list>
            <single_particle_preparation preparation_id="1">
               <concentration units="mg/mL">0.15</concentration>
               <buffer>
                  <ph>7.5</ph>
                  <details>polymix buffer</details>
               </buffer>
               <staining>
                  <type>NEGATIVE</type>
                  <details>no staining, cryo-EM with holey carbon grids</details>
               </staining>
               <vitrification>
                  <cryogen_name>ETHANE</cryogen_name>
                  <chamber_humidity units="percentage">45</chamber_humidity>
                  <chamber_temperature units="K">20</chamber_temperature>
                  <instrument>HOMEMADE PLUNGER</instrument>
                  <details>Vitrification instrument: home-made cryo-plunger</details>
                  <method>blot for 2 seconds before plunging</method>
               </vitrification>
            </single_particle_preparation>
         </specimen_preparation_list>
         <microscopy_list>
            <single_particle_microscopy microscopy_id="1">
               <microscope>FEI/PHILIPS CM200FEG/ST</microscope>
               <illumination_mode>FLOOD BEAM</illumination_mode>
               <imaging_mode>BRIGHT FIELD</imaging_mode>
               <electron_source>FIELD EMISSION GUN</electron_source>
               <acceleration_voltage units="kV">200</acceleration_voltage>
               <nominal_cs units="mm">2.1</nominal_cs>
               <nominal_defocus_min units="&#181;m">0.5</nominal_defocus_min>
               <nominal_defocus_max units="&#181;m">2.9</nominal_defocus_max>
               <nominal_magnification>50000.0</nominal_magnification>
               <calibrated_magnification>48000.0</calibrated_magnification>
               <specimen_holder_model>GATAN LIQUID NITROGEN</specimen_holder_model>
               <temperature>
                  <temperature_min units="K">100</temperature_min>
                  <temperature_max units="K">102</temperature_max>
                  <temperature_average units="K">100</temperature_average>
               </temperature>
               <date>2001-09-06</date>
               <image_recording_list>
                  <image_recording>
                     <film_or_detector_model category="FILM">KODAK SO-163 FILM</film_or_detector_model>
                     <digitization_details>
                        <scanner>PATCHWORK DENSITOMETER</scanner>
                        <sampling_interval units="&#181;m">3</sampling_interval>
                     </digitization_details>
                     <number_real_images>78</number_real_images>
                     <average_electron_dose_per_image units="e/&#8491;^2">10</average_electron_dose_per_image>
                     <bits_per_pixel>12.</bits_per_pixel>
                  </image_recording>
               </image_recording_list>
               <specimen_holder>Side entry liquid nitrogen-cooled cryo specimen holder.</specimen_holder>
            </single_particle_microscopy>
         </microscopy_list>
         <singleparticle_processing image_processing_id="1">
            <ctf_correction>
               <details>each particle</details>
            </ctf_correction>
            <final_reconstruction>
               <applied_symmetry>
                  <point_group>C1</point_group>
               </applied_symmetry>
               <algorithm>OTHER</algorithm>
               <resolution res_type="BY AUTHOR" units="&#8491;">14.0</resolution>
               <resolution_method>OTHER</resolution_method>
               <software_list>
                  <software>
                     <name>IMAGIC</name>
                  </software>
               </software_list>
               <details>exact filtered back-projection</details>
               <number_images_used>15800</number_images_used>
            </final_reconstruction>
            <final_angle_assignment>
               <details>beta gamma</details>
            </final_angle_assignment>
            <final_two_d_classification>
               <number_classes>103</number_classes>
            </final_two_d_classification>
         </singleparticle_processing>
      </structure_determination>
   </structure_determination_list>
   <map format="CCP4" size_kbytes="6751">
      <file>emd_1005.map.gz</file>
      <symmetry>
         <space_group>1</space_group>
      </symmetry>
      <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
      <dimensions>
         <col>120</col>
         <row>120</row>
         <sec>120</sec>
      </dimensions>
      <origin>
         <col>-60</col>
         <row>-60</row>
         <sec>-60</sec>
      </origin>
      <spacing>
         <x>120</x>
         <y>120</y>
         <z>120</z>
      </spacing>
      <cell>
         <a units="&#8491;">290.28</a>
         <b units="&#8491;">290.28</b>
         <c units="&#8491;">290.28</c>
         <alpha units="deg">90</alpha>
         <beta units="deg">90</beta>
         <gamma units="deg">90</gamma>
      </cell>
      <axis_order>
         <fast>X</fast>
         <medium>Y</medium>
         <slow>Z</slow>
      </axis_order>
      <statistics>
         <minimum>-0.159669</minimum>
         <maximum>0.213811</maximum>
         <average>-0.000130684</average>
         <std>0.0224271</std>
      </statistics>
      <pixel_spacing>
         <x units="&#8491;">2.419</x>
         <y units="&#8491;">2.419</y>
         <z units="&#8491;">2.419</z>
      </pixel_spacing>
      <contour_list>
         <contour primary="true">
            <level>0.0401</level>
         </contour>
      </contour_list>
      <annotation_details>E. coli ribosomal termination
        complex       with release factor RF2.</annotation_details>
      <details>::::EMDATABANK.org::::EMD-1005::::</details>
   </map>
   <interpretation>
      <modelling_list>
         <modelling>
            <initial_model>
               <access_code>1GIX</access_code>
            </initial_model>
            <refinement_protocol>RIGID BODY FIT</refinement_protocol>
            <software_list>
               <software>
                  <name>eye</name>
               </software>
            </software_list>
            <details>Protocol: rigid body. rigid body of three individual domains keeping the connectivity; linkers betweenn domains defined based on temperature factors of crystal structure, conserved Gly and Pro residues, proteolytic sites, and global domain architecture</details>
            <target_criteria>best visual fit using the program O</target_criteria>
            <refinement_space>REAL</refinement_space>
         </modelling>
         <modelling>
            <initial_model>
               <access_code>1GIY</access_code>
            </initial_model>
            <refinement_protocol>RIGID BODY FIT</refinement_protocol>
            <software_list>
               <software>
                  <name>eye</name>
               </software>
            </software_list>
            <details>Protocol: rigid body. rigid body of three individual domains keeping the connectivity; linkers betweenn domains defined based on temperature factors of crystal structure, conserved Gly and Pro residues, proteolytic sites, and global domain architecture</details>
            <target_criteria>best visual fit using the program O</target_criteria>
            <refinement_space>REAL</refinement_space>
         </modelling>
      </modelling_list>
   </interpretation>
</emd>