<emd xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" emdb_id="EMD-1083" 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>2004-05-18</deposition>
         <header_release>2004-06-05</header_release>
         <map_release>2005-05-25</map_release>
         <update>2012-10-17</update>
      </key_dates>
      <title>The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes.</title>
      <authors_list>
         <author>Huiskonen JT</author>
         <author>Kivela HM</author>
         <author>Bamford DH</author>
         <author>Butcher SJ</author>
      </authors_list>
      <keywords>
         </keywords>
   </admin>
   <crossreferences>
      <citation_list>
         <primary_citation>
            <journal_citation published="true">
               <author order="1">Huiskonen JT</author>
               <author order="2">Kivela HM</author>
               <author order="3">Bamford DH</author>
               <author order="4">Butcher SJ</author>
               <title>The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes.</title>
               <journal>NAT.STRUCT.MOL.BIOL.</journal>
               <volume>11</volume>
               <first_page>850</first_page>
               <last_page>856</last_page>
               <year>2004</year>
               <external_references type="PUBMED">15286721</external_references>
               <external_references type="DOI">doi:10.1038/nsmb807</external_references>
            </journal_citation>
         </primary_citation>
      </citation_list>
   </crossreferences>
   <sample>
      <name>PM2 virion</name>
      <supramolecule_list>
         <sample_supramolecule supramolecule_id="1000">
            <name>PM2 virion</name>
            <details>Purified virion was purified, pelleted and
      resuspended just prior to       application to the grid.</details>
            <number_unique_components>1</number_unique_components>
            <molecular_weight>
               <theoretical units="MDa">33.8</theoretical>
               <method>Reported mass of the whole virion in the
      literature is       47 MDa, 72 percent of which is protein.</method>
            </molecular_weight>
         </sample_supramolecule>
         <virus_supramolecule supramolecule_id="1">
            <name synonym="PM2">Pseudoalteromonas phage PM2</name>
            <details>includes mass of DNA, lipid and protein</details>
            <sci_species_name ncbi="10661">Pseudoalteromonas phage PM2</sci_species_name>
            <natural_host database="NCBI">
               <organism ncbi="96059">Pseudoalteromonas sp. ER72M2</organism>
               <synonym_organism>BACTERIA(EUBACTERIA)</synonym_organism>
            </natural_host>
            <host_system database="NCBI">
               </host_system>
            <molecular_weight>
               <experimental units="MDa">47</experimental>
            </molecular_weight>
            <virus_shell shell_id="1">
               <name>P2</name>
               <diameter units="&#8491;">597</diameter>
               <triangulation>21</triangulation>
            </virus_shell>
            <virus_type>VIRION</virus_type>
            <virus_isolate>STRAIN</virus_isolate>
            <virus_enveloped>true</virus_enveloped>
            <virus_empty>false</virus_empty>
            <syn_species_name>PM2</syn_species_name>
         </virus_supramolecule>
      </supramolecule_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">4</concentration>
               <buffer>
                  <ph>7.2</ph>
                  <details>CaCl2, 5mM  Tris-HCl, 10-20 mM  NaCl, 25-125 mM</details>
               </buffer>
               <grid>
                  <details>400 mesh copper grid, R2/2 quantifoil holey</details>
               </grid>
               <vitrification>
                  <cryogen_name>ETHANE</cryogen_name>
                  <chamber_temperature units="K">90</chamber_temperature>
                  <instrument>HOMEMADE PLUNGER</instrument>
                  <details>Vitrification instrument: EMBL design</details>
                  <method>A small vial of ethane  is placed inside a         larger
        liquid       nitrogen reservoir. The grid holding         3
        microliters of the sample       is held in place at         the
        bottom       of a plunger by the means of fine         tweezers.
        When the       liquid ethane is ready, a piece         of
        filter       paper       is then       pressed         against
        the       sample to       blot       off excess buffer,
        sufficient to       leave a thin layer       on       the grid.
        The       filter paper       is       removed, and the
        plunger is       allowed to drop       into the       liquid
        ethane.       Once       the grid       enters the liquid
        ethane,       the sample is       rapidly       frozen, and the
        grid is       transferred under liquid       nitrogen       to a
        storage box       immersed in liquid       nitrogen for later
        use in the microscope.</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">0.7</nominal_defocus_min>
               <nominal_defocus_max units="&#181;m">4.4</nominal_defocus_max>
               <nominal_magnification>50000.0</nominal_magnification>
               <specimen_holder_model>GATAN LIQUID NITROGEN</specimen_holder_model>
               <temperature>
                  <temperature_min units="K">90</temperature_min>
                  <temperature_max units="K">94</temperature_max>
                  <temperature_average units="K">93</temperature_average>
               </temperature>
               <alignment_procedure>
                  <legacy>
                     <astigmatism>objective lens astigmatism was corrected at</astigmatism>
                  </legacy>
               </alignment_procedure>
               <details>A box anticontaminator was fitted with a         minimum
        achievable       temperature of 88 K</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>72</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">
            <details>The particles were first automatically selected using
          ETHAN, and then  boxed out manually in EMAN.</details>
            <ctf_correction>
               <details>each particle, wiener factor 0.1</details>
            </ctf_correction>
            <final_reconstruction>
               <applied_symmetry>
                  <point_group>I</point_group>
               </applied_symmetry>
               <algorithm>OTHER</algorithm>
               <resolution res_type="BY AUTHOR" units="&#8491;">12.3</resolution>
               <resolution_method>FSC 0.5 CUT-OFF</resolution_method>
               <software_list>
                  <software>
                     <name>EMBL, P3DR</name>
                  </software>
               </software_list>
               <number_images_used>5284</number_images_used>
            </final_reconstruction>
         </singleparticle_processing>
      </structure_determination>
   </structure_determination_list>
   <map format="CCP4" size_kbytes="67049">
      <file>emd_1083.map.gz</file>
      <symmetry>
         <space_group>1</space_group>
      </symmetry>
      <data_type>IMAGE STORED AS SIGNED INTEGER (2 BYTES)</data_type>
      <dimensions>
         <col>325</col>
         <row>325</row>
         <sec>325</sec>
      </dimensions>
      <origin>
         <col>0</col>
         <row>0</row>
         <sec>0</sec>
      </origin>
      <spacing>
         <x>325</x>
         <y>325</y>
         <z>325</z>
      </spacing>
      <cell>
         <a units="&#8491;">910</a>
         <b units="&#8491;">910</b>
         <c units="&#8491;">910</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>-2979.0</minimum>
         <maximum>5398.0</maximum>
         <average>0.0460828</average>
         <std>680.032000000000039</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>1190.0</level>
         </contour>
      </contour_list>
      <annotation_details>This map was used for difference imaging with
      the       proteinase K- and bromelain-treated virus
      reconstructions to       determine the  domain structure of
      the receptor binding protein.</annotation_details>
      <details>::::EMDATABANK.org::::EMD-1083::::</details>
   </map>
</emd>