<emd xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" emdb_id="EMD-1981" 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>2011-11-06</deposition>
         <header_release>2011-12-16</header_release>
         <map_release>2011-12-21</map_release>
         <update>2012-02-03</update>
      </key_dates>
      <title>Asymmetric cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozyme</title>
      <authors_list>
         <author>Malet H</author>
         <author>Canellas F</author>
         <author>Sawa J</author>
         <author>Yan J</author>
         <author>Thalassinos K</author>
         <author>Ehrmann M</author>
         <author>Clausen T</author>
         <author>Saibil HR</author>
      </authors_list>
      <keywords>Chaperone, Protease</keywords>
   </admin>
   <crossreferences>
      <citation_list>
         <primary_citation>
            <journal_citation published="true">
               <author order="1">Malet H</author>
               <author order="2">Canellas F</author>
               <author order="3">Sawa J</author>
               <author order="4">Yan J</author>
               <author order="5">Thalassinos K</author>
               <author order="6">Ehrmann M</author>
               <author order="7">Clausen T</author>
               <author order="8">Saibil HR</author>
               <title>Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.</title>
               <journal>NAT.STRUCT.MOL.BIOL.</journal>
               <volume>19</volume>
               <first_page>152</first_page>
               <last_page>157</last_page>
               <year>2012</year>
               <external_references type="PUBMED">22245966</external_references>
               <external_references type="DOI">doi:10.1038/nsmb.2210</external_references>
            </journal_citation>
         </primary_citation>
      </citation_list>
      <pdb_list>
         <pdb_reference>
            <pdb_id>4a8a</pdb_id>
            <relationship>
               <in_frame>FULLOVERLAP</in_frame>
            </relationship>
         </pdb_reference>
      </pdb_list>
   </crossreferences>
   <sample>
      <name>Escherichia coli DegQ
Gallus gallus lysozyme</name>
      <supramolecule_list>
         <sample_supramolecule supramolecule_id="1000">
            <name>Escherichia coli DegQ
Gallus gallus lysozyme</name>
            <oligomeric_state>Six lysozyme monomers bind to one DegQ 12-mer</oligomeric_state>
            <number_unique_components>2</number_unique_components>
            <molecular_weight>
               <experimental units="MDa">0.625</experimental>
               <theoretical units="MDa">0.625</theoretical>
               <method>Native mass spectrometry Size elution chromatography</method>
            </molecular_weight>
         </sample_supramolecule>
      </supramolecule_list>
      <macromolecule_list>
         <protein_or_peptide macromolecule_id="1">
            <name synonym="DegQ">DegQ</name>
            <natural_source database="NCBI">
               <organism ncbi="562">Escherichia coli</organism>
               <strain>K-12</strain>
               <cell>Escherichia coli</cell>
               <cellular_location>Periplasm</cellular_location>
            </natural_source>
            <molecular_weight>
               <experimental units="MDa">0.045</experimental>
               <theoretical units="MDa">0.045</theoretical>
            </molecular_weight>
            <number_of_copies>12</number_of_copies>
            <oligomeric_state>Dodecamer</oligomeric_state>
            <recombinant_exp_flag>true</recombinant_exp_flag>
            <recombinant_expression database="NCBI">
               <recombinant_organism ncbi="562">Escherichia coli</recombinant_organism>
               <recombinant_plasmid>pET26b</recombinant_plasmid>
            </recombinant_expression>
            <sequence>
               </sequence>
         </protein_or_peptide>
         <protein_or_peptide macromolecule_id="2">
            <name synonym="Lysozyme">Lysozyme</name>
            <natural_source database="NCBI">
               <organism ncbi="9031">Gallus gallus</organism>
               <synonym_organism>Chicken</synonym_organism>
               <tissue>Egg white</tissue>
            </natural_source>
            <molecular_weight>
               <experimental units="MDa">0.0143</experimental>
               <theoretical units="MDa">0.0143</theoretical>
            </molecular_weight>
            <number_of_copies>6</number_of_copies>
            <oligomeric_state>Monomer</oligomeric_state>
            <recombinant_exp_flag>false</recombinant_exp_flag>
            <recombinant_expression database="NCBI">
               </recombinant_expression>
            <sequence>
               <external_references type="GO">GO:0003796</external_references>
               <external_references type="INTERPRO">IPR002152</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">0.2</concentration>
               <buffer>
                  <ph>7.5</ph>
                  <details>20 mM HEPES/NaOH, 150 mM NaCl</details>
               </buffer>
               <grid>
                  <details>C-flat grids (CF-2/2-4C-100 Protochips)</details>
               </grid>
               <vitrification>
                  <cryogen_name>ETHANE</cryogen_name>
                  <instrument>HOMEMADE PLUNGER</instrument>
                  <details>Vitrification instrument: Manual 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 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">1.0</nominal_defocus_min>
               <nominal_defocus_max units="&#181;m">3.0</nominal_defocus_max>
               <nominal_magnification>50000.0</nominal_magnification>
               <calibrated_magnification>50000.0</calibrated_magnification>
               <specimen_holder_model>GATAN LIQUID NITROGEN</specimen_holder_model>
               <temperature>
                  <temperature_min units="K">90</temperature_min>
                  <temperature_max units="K">92</temperature_max>
                  <temperature_average units="K">91</temperature_average>
               </temperature>
               <alignment_procedure>
                  <legacy>
                     <astigmatism>objective lens astigmatism was corrected at 150,000 times magnification</astigmatism>
                     <electron_beam_tilt_params>0</electron_beam_tilt_params>
                  </legacy>
               </alignment_procedure>
               <details>Low dose mode</details>
               <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">7</sampling_interval>
                     </digitization_details>
                     <number_real_images>100</number_real_images>
                     <average_electron_dose_per_image units="e/&#8491;^2">15</average_electron_dose_per_image>
                     <bits_per_pixel>8.</bits_per_pixel>
                  </image_recording>
               </image_recording_list>
               <specimen_holder>Single tilt cryo</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>Phase flipping</details>
            </ctf_correction>
            <final_reconstruction>
               <applied_symmetry>
                  <point_group>C1</point_group>
               </applied_symmetry>
               <algorithm>OTHER</algorithm>
               <resolution res_type="BY AUTHOR" units="&#8491;">14.2</resolution>
               <resolution_method>FSC 0.5 CUT-OFF</resolution_method>
               <software_list>
                  <software>
                     <name>IMAGIC-5, SPIDER</name>
                  </software>
               </software_list>
               <number_images_used>13432</number_images_used>
            </final_reconstruction>
         </singleparticle_processing>
      </structure_determination>
   </structure_determination_list>
   <map format="CCP4" size_kbytes="8193">
      <file>emd_1981.map.gz</file>
      <symmetry>
         <space_group>1</space_group>
      </symmetry>
      <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
      <dimensions>
         <col>128</col>
         <row>128</row>
         <sec>128</sec>
      </dimensions>
      <origin>
         <col>-64</col>
         <row>-64</row>
         <sec>-64</sec>
      </origin>
      <spacing>
         <x>128</x>
         <y>128</y>
         <z>128</z>
      </spacing>
      <cell>
         <a units="&#8491;">358.4</a>
         <b units="&#8491;">358.4</b>
         <c units="&#8491;">358.4</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>-2.79762</minimum>
         <maximum>40.962499999999999</maximum>
         <average>-0.00000476495</average>
         <std>1.00186</std>
      </statistics>
      <pixel_spacing>
         <x units="&#8491;">2.8</x>
         <y units="&#8491;">2.8</y>
         <z units="&#8491;">2.8</z>
      </pixel_spacing>
      <contour_list>
         <contour primary="true">
            <level>0.2</level>
            <source>AUTHOR</source>
         </contour>
      </contour_list>
      <annotation_details>Asymmetric cryo-EM map of E. coli DegQ 12-mer in complex with lysozyme</annotation_details>
      <details>::::EMDATABANK.org::::EMD-1981::::</details>
   </map>
   <interpretation>
      <modelling_list>
         <modelling>
            <initial_model>
               <access_code>3STJ</access_code>
               <chain>
                  <chain_id>A</chain_id>
               </chain>
               <chain>
                  <chain_id>B</chain_id>
               </chain>
               <chain>
                  <chain_id>C</chain_id>
               </chain>
            </initial_model>
            <refinement_protocol>FLEXIBLE FIT</refinement_protocol>
            <software_list>
               <software>
                  <name>Chimera, Flex-EM</name>
               </software>
            </software_list>
            <details>PDBEntryID_givenInChain. Protocol: Rigid body and flexible fitting. Protease and PDZ1 trimers extracted from 3STJ pdb entry. PDZ2 domain modelled with MODELLER from E. coli DegP pdb entry 3CS0.</details>
            <target_criteria>Cross-correlation, energy</target_criteria>
            <refinement_space>REAL</refinement_space>
         </modelling>
         <modelling>
            <initial_model>
               <access_code>1DPX</access_code>
               <chain>
                  <chain_id>A</chain_id>
               </chain>
            </initial_model>
            <refinement_protocol>RIGID BODY FIT</refinement_protocol>
            <software_list>
               <software>
                  <name>Flex-EM</name>
               </software>
            </software_list>
            <details>PDBEntryID_givenInChain. Protocol: Rigid body</details>
            <target_criteria>Cross-correlation, energy</target_criteria>
            <refinement_space>REAL</refinement_space>
         </modelling>
      </modelling_list>
   </interpretation>
</emd>