<emd xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" emdb_id="EMD-1055" 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>2003-09-22</deposition>
         <header_release>2003-09-29</header_release>
         <map_release>2004-01-06</map_release>
         <update>2013-12-04</update>
      </key_dates>
      <title>Locking and unlocking of ribosomal motions.</title>
      <authors_list>
         <author>Valle M</author>
         <author>Zavialov A</author>
         <author>Li W</author>
         <author>Stagg SM</author>
         <author>Sengupta J</author>
         <author>Nielsen RC</author>
         <author>Nissen P</author>
         <author>Hervey SC</author>
         <author>Ehrenberg M</author>
         <author>Frank J</author>
      </authors_list>
      <keywords>
         </keywords>
   </admin>
   <crossreferences>
      <citation_list>
         <primary_citation>
            <journal_citation published="true">
               <author order="1">Valle M</author>
               <author order="2">Zavialov A</author>
               <author order="3">Li W</author>
               <author order="4">Stagg SM</author>
               <author order="5">Sengupta J</author>
               <author order="6">Nielsen RC</author>
               <author order="7">Nissen P</author>
               <author order="8">Harvey SC</author>
               <author order="9">Ehrenberg M</author>
               <author order="10">Frank J</author>
               <title>Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy.</title>
               <journal>NAT.STRUCT.MOL.BIOL.</journal>
               <volume>10</volume>
               <first_page>899</first_page>
               <last_page>906</last_page>
               <year>2003</year>
               <external_references type="PUBMED">14566331</external_references>
               <external_references type="DOI">doi:10.1038/nsb1003</external_references>
            </journal_citation>
         </primary_citation>
      </citation_list>
      <pdb_list>
         <pdb_reference>
            <pdb_id>1qza</pdb_id>
            <relationship>
               <in_frame>FULLOVERLAP</in_frame>
            </relationship>
         </pdb_reference>
         <pdb_reference>
            <pdb_id>1qzd</pdb_id>
            <relationship>
               <in_frame>FULLOVERLAP</in_frame>
            </relationship>
         </pdb_reference>
         <pdb_reference>
            <pdb_id>1r2x</pdb_id>
            <relationship>
               <in_frame>FULLOVERLAP</in_frame>
            </relationship>
         </pdb_reference>
      </pdb_list>
   </crossreferences>
   <sample>
      <name>70S ribosome from E. coli complex 70S-fMet-tRNA-Phe-tRNA-EF-Tu-GDP-kirromycin.</name>
      <supramolecule_list>
         <sample_supramolecule supramolecule_id="1000">
            <name>70S ribosome from E. coli complex 70S-fMet-tRNA-Phe-tRNA-EF-Tu-GDP-kirromycin.</name>
            <number_unique_components>5</number_unique_components>
         </sample_supramolecule>
         <complex_supramolecule supramolecule_id="1">
            <name synonym="ribosome">70S from E. coli</name>
            <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>
            <ribosome-details>ribosome-prokaryote: ALL</ribosome-details>
         </complex_supramolecule>
      </supramolecule_list>
      <macromolecule_list>
         <rna macromolecule_id="1">
            <name synonym="trna">fMet-tRNAfMet</name>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
            </natural_source>
            <classification>OTHER</classification>
            <structure>DOUBLE HELIX</structure>
            <synthetic_flag>false</synthetic_flag>
         </rna>
         <rna macromolecule_id="2">
            <name synonym="trna">Phe-tRNAPhe</name>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
            </natural_source>
            <classification>OTHER</classification>
            <structure>DOUBLE HELIX</structure>
            <synthetic_flag>false</synthetic_flag>
         </rna>
         <protein_or_peptide macromolecule_id="3">
            <name synonym="Elongation Factor">Elongation Factor Tu</name>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
            </natural_source>
            <number_of_copies>1</number_of_copies>
            <recombinant_exp_flag>false</recombinant_exp_flag>
            <recombinant_expression database="NCBI">
               </recombinant_expression>
            <sequence>
               </sequence>
         </protein_or_peptide>
         <rna macromolecule_id="4">
            <name synonym="trna">deacylated tRNA</name>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
            </natural_source>
            <classification>OTHER</classification>
            <structure>DOUBLE HELIX</structure>
            <synthetic_flag>false</synthetic_flag>
         </rna>
      </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">
               <buffer>
                  <ph>7.5</ph>
                  <details>5 mM potassium phosphate, 5 mM magnesium
          acetate,       5 mM       ammonium chloride, 95 mM potassium
          chloride,       0.5 mM calcium       chloride, 8 mM
          putrescine, 1 mM       spermidine, and 1 mM dithioerythritol</details>
               </buffer>
               <staining>
                  <type>NEGATIVE</type>
                  <details>Cryo-electron microscopy. No stain.</details>
               </staining>
               <grid>
                  <details>300 mesh Quantifoil R2/4</details>
               </grid>
               <vitrification>
                  <cryogen_name>ETHANE</cryogen_name>
                  <chamber_temperature units="K">90</chamber_temperature>
                  <method>two-face blotting for 1 second</method>
               </vitrification>
            </single_particle_preparation>
         </specimen_preparation_list>
         <microscopy_list>
            <single_particle_microscopy microscopy_id="1">
               <microscope>FEI TECNAI F20</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</nominal_cs>
               <nominal_defocus_min units="&#181;m">2.0</nominal_defocus_min>
               <nominal_defocus_max units="&#181;m">4.0</nominal_defocus_max>
               <nominal_magnification>50000.0</nominal_magnification>
               <calibrated_magnification>49650.0</calibrated_magnification>
               <specimen_holder_model>GATAN LIQUID NITROGEN</specimen_holder_model>
               <temperature>
                  <temperature_average units="K">90</temperature_average>
               </temperature>
               <alignment_procedure>
                  <legacy>
                     <astigmatism>corrected at 175,000</astigmatism>
                  </legacy>
               </alignment_procedure>
               <image_recording_list>
                  <image_recording>
                     <film_or_detector_model category="FILM">KODAK SO-163 FILM</film_or_detector_model>
                     <digitization_details>
                        <scanner>ZEISS SCAI</scanner>
                        <sampling_interval units="&#181;m">14</sampling_interval>
                     </digitization_details>
                     <number_real_images>50</number_real_images>
                     <average_electron_dose_per_image units="e/&#8491;^2">15</average_electron_dose_per_image>
                     <od_range>1.0</od_range>
                     <bits_per_pixel>16.</bits_per_pixel>
                  </image_recording>
               </image_recording_list>
               <specimen_holder>single tilt cryoholder</specimen_holder>
               <tilt_angle_min>0</tilt_angle_min>
               <tilt_angle_max>0</tilt_angle_max>
            </single_particle_microscopy>
         </microscopy_list>
         <singleparticle_processing image_processing_id="1">
            <ctf_correction>
               <details>segregation in defocus groups and correction
        in volumes</details>
            </ctf_correction>
            <final_reconstruction>
               <applied_symmetry>
                  <point_group>C1</point_group>
               </applied_symmetry>
               <algorithm>OTHER</algorithm>
               <resolution res_type="BY AUTHOR" units="&#8491;">9.0</resolution>
               <resolution_method>OTHER</resolution_method>
               <software_list>
                  <software>
                     <name>Spider</name>
                  </software>
               </software_list>
               <number_images_used>75996</number_images_used>
            </final_reconstruction>
         </singleparticle_processing>
      </structure_determination>
   </structure_determination_list>
   <map format="CCP4" size_kbytes="8584">
      <file>emd_1055.map.gz</file>
      <symmetry>
         <space_group>1</space_group>
      </symmetry>
      <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
      <dimensions>
         <col>130</col>
         <row>130</row>
         <sec>130</sec>
      </dimensions>
      <origin>
         <col>-65</col>
         <row>-65</row>
         <sec>-65</sec>
      </origin>
      <spacing>
         <x>130</x>
         <y>130</y>
         <z>130</z>
      </spacing>
      <cell>
         <a units="&#8491;">366.6</a>
         <b units="&#8491;">366.6</b>
         <c units="&#8491;">366.6</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>-85.858900000000006</minimum>
         <maximum>250.984000000000009</maximum>
         <average>4.44442</average>
         <std>25.344000000000001</std>
      </statistics>
      <pixel_spacing>
         <x units="&#8491;">2.82</x>
         <y units="&#8491;">2.82</y>
         <z units="&#8491;">2.82</z>
      </pixel_spacing>
      <contour_list>
         <contour primary="true">
            <level>57.200000000000003</level>
         </contour>
      </contour_list>
      <annotation_details>70S + fMet-tRNA + PhetRNA + EF-Tu + GDP + kir
      mRNA codes for MP-stop</annotation_details>
      <details>::::EMDATABANK.org::::EMD-1055::::</details>
   </map>
   <interpretation>
      <modelling_list>
         <modelling>
            <initial_model>
               <access_code>1FNM</access_code>
            </initial_model>
            <initial_model>
               <access_code>1FFK</access_code>
            </initial_model>
            <initial_model>
               <access_code>1FJF</access_code>
            </initial_model>
            <refinement_protocol>RIGID BODY FIT</refinement_protocol>
            <software_list>
               <software>
                  <name>O</name>
               </software>
            </software_list>
            <details>Protocol: rigid body. Manual fitting in O.The docking of X-ray structures into the cryo-EM maps was made using O and the visualization was performed in IRIS Explorer. EF-G domains were taken from the Thermus thermophilus H573A mutant crystal structure in complex with GDP (PDB code: 1FNM). The coordinates of the ribosomal proteins and rRNAs were taken from published atomic structures (PDB code 1FFK for the 50S subunit; 1FJF for the 30S subunit and the docking was performed using the coordinates as rigid bodies.</details>
            <target_criteria>correlation coeficient</target_criteria>
         </modelling>
      </modelling_list>
   </interpretation>
</emd>