<emd emdb_id="EMD-1088" version="3.0.1.1" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" 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>2004-07-01</deposition>
            <header_release>2004-07-07</header_release>
            <map_release>2004-09-07</map_release>
            <update>2013-09-25</update>
        </key_dates>
        <title>Structure of the acrosomal bundle.</title>
        <authors_list>
            <author>Schmid MF</author>
            <author>Sherman MB</author>
            <author>Matsudaira P</author>
            <author>Chiu W</author>
        </authors_list>
        <keywords />
    </admin>
    <crossreferences>
        <citation_list>
            <primary_citation>
                <journal_citation published="true">
                    <author order="1">Schmid MF</author>
                    <author order="2">Sherman MB</author>
                    <author order="3">Matsudaira P</author>
                    <author order="4">Chiu W</author>
                    <title>Structure of the acrosomal bundle.</title>
                    <journal>NATURE</journal>
                    <volume>431</volume>
                    <first_page>104</first_page>
                    <last_page>107</last_page>
                    <year>2004</year>
                    <external_references type="PUBMED">15343340</external_references>
                    <external_references type="DOI">doi:10.1038/nature02881</external_references>
                </journal_citation>
            </primary_citation>
        </citation_list>
        <pdb_list>
            <pdb_reference>
                <pdb_id>3b5u</pdb_id>
                <relationship>
                    <in_frame>FULLOVERLAP</in_frame>
                </relationship>
            </pdb_reference>
            <pdb_reference>
                <pdb_id>3b63</pdb_id>
                <relationship>
                    <in_frame>FULLOVERLAP</in_frame>
                </relationship>
            </pdb_reference>
        </pdb_list>
    </crossreferences>
    <sample>
        <name>Acrosomal bundle from Limulus sperm</name>
        <supramolecule_list>
            <sample_supramolecule supramolecule_id="1000">
                <name>Acrosomal bundle from Limulus sperm</name>
                <oligomeric_state>helix of actin and  scruin in a 1 to 1 stoichiometry</oligomeric_state>
                <number_unique_components>2</number_unique_components>
                <molecular_weight>
                    <experimental units="MDa">4.2</experimental>
                    <theoretical units="MDa">4.2</theoretical>
                    <method>calculated from molecular weight</method>
                </molecular_weight>
            </sample_supramolecule>
        </supramolecule_list>
        <macromolecule_list>
            <protein_or_peptide macromolecule_id="1">
                <name synonym="F-actin">actin</name>
                <natural_source database="NCBI">
                    <organism ncbi="6850">Limulus polyphemus</organism>
                    <synonym_organism>horseshoe crab</synonym_organism>
                    <tissue>sperm</tissue>
                    <cell>sperm</cell>
                    <organelle>acrosomal process</organelle>
                    <cellular_location>acrosomal bundle</cellular_location>
                </natural_source>
                <molecular_weight>
                    <experimental units="MDa">1.176</experimental>
                    <theoretical units="MDa">1.176</theoretical>
                </molecular_weight>
                <details>28 of these per unit cell</details>
                <number_of_copies>28</number_of_copies>
                <oligomeric_state>helical</oligomeric_state>
                <recombinant_exp_flag>false</recombinant_exp_flag>
                <recombinant_expression database="NCBI" />
                <sequence />
            </protein_or_peptide>
            <protein_or_peptide macromolecule_id="2">
                <name synonym="scruin">scruin</name>
                <natural_source database="NCBI">
                    <organism ncbi="6850">Limulus polyphemus</organism>
                    <synonym_organism>horseshoe crab</synonym_organism>
                    <tissue>sperm</tissue>
                    <cell>sperm</cell>
                    <organelle>acrosomal process</organelle>
                    <cellular_location>acrosomal bundle</cellular_location>
                </natural_source>
                <molecular_weight>
                    <experimental units="MDa">3.08</experimental>
                    <theoretical units="MDa">3.08</theoretical>
                </molecular_weight>
                <details>28 of these per unit cell</details>
                <number_of_copies>28</number_of_copies>
                <oligomeric_state>helical</oligomeric_state>
                <recombinant_exp_flag>false</recombinant_exp_flag>
                <recombinant_expression database="NCBI" />
                <sequence />
            </protein_or_peptide>
        </macromolecule_list>
    </sample>
    <structure_determination_list>
        <structure_determination structure_determination_id="1">
            <method>helical</method>
            <aggregation_state>twoDArray</aggregation_state>
            <specimen_preparation_list>
                <helical_preparation preparation_id="1">
                    <concentration units="mg/mL">10</concentration>
                    <buffer>
                        <ph>7.4</ph>
                        <details>see J Mol Biol, 221: 711-725 (1991)</details>
                    </buffer>
                    <vitrification>
                        <cryogen_name>ETHANE</cryogen_name>
                        <chamber_humidity units="percentage">100</chamber_humidity>
                        <chamber_temperature units="K">90</chamber_temperature>
                        <instrument>HOMEMADE PLUNGER</instrument>
                        <details>Vitrification instrument: homemade guillotine</details>
                    </vitrification>
                    <details>naturally occurring intracellular ordered array.
Space group is P2sub1 or P1 21 1. P 1 21 refers to a 2-fold screw axis in the plane of the 2D crystal, whereas I have defined the 2-fold screw along z (second setting monoclinic).</details>
                </helical_preparation>
            </specimen_preparation_list>
            <microscopy_list>
                <helical_microscopy microscopy_id="1">
                    <microscope>JEOL 4000EX</microscope>
                    <illumination_mode>FLOOD BEAM</illumination_mode>
                    <imaging_mode>BRIGHT FIELD</imaging_mode>
                    <electron_source>LAB6</electron_source>
                    <acceleration_voltage units="kV">400</acceleration_voltage>
                    <nominal_defocus_min units="&#181;m">0.8</nominal_defocus_min>
                    <nominal_defocus_max units="&#181;m">3.0</nominal_defocus_max>
                    <nominal_magnification>40000.0</nominal_magnification>
                    <specimen_holder_model>GATAN LIQUID NITROGEN</specimen_holder_model>
                    <temperature>
                        <temperature_average units="K">90</temperature_average>
                    </temperature>
                    <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>90</number_real_images>
                            <average_electron_dose_per_image units="e/&#8491;^2">15</average_electron_dose_per_image>
                            <details>153 bundles selected</details>
                            <od_range>1.5</od_range>
                        </image_recording>
                    </image_recording_list>
                    <specimen_holder>side entry</specimen_holder>
                </helical_microscopy>
            </microscopy_list>
            <helical_processing image_processing_id="1">
                <final_reconstruction>
                    <algorithm>OTHER</algorithm>
                    <resolution res_type="BY AUTHOR" units="&#8491;">9.5</resolution>
                    <resolution_method>OTHER</resolution_method>
                    <software_list>
                        <software>
                            <name>MRC, CCP4, homemade</name>
                        </software>
                    </software_list>
                    <details>1000 2 unit cell segments from 153 bundles       (ref:Schmid,
        MF,       J,.       Struct Biol. 2003, 144:195-208.</details>
                </final_reconstruction>
                <ctf_correction>
                    <details>each bundle</details>
                </ctf_correction>
                <crystal_parameters>
                    <unit_cell>
                        <a units="&#8491;">145</a>
                        <b units="&#8491;">145</b>
                        <c units="&#8491;">765</c>
                        <gamma units="deg">120</gamma>
                        <alpha units="deg">90</alpha>
                        <beta units="deg">90</beta>
                    </unit_cell>
                    <plane_group>P 1 21</plane_group>
                </crystal_parameters>
            </helical_processing>
        </structure_determination>
    </structure_determination_list>
    <map format="CCP4" size_kbytes="48385">
        <file>emd_1088.map.gz</file>
        <symmetry>
            <space_group>1</space_group>
        </symmetry>
        <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
        <dimensions>
            <col>576</col>
            <row>192</row>
            <sec>112</sec>
        </dimensions>
        <origin>
            <col>-288</col>
            <row>-96</row>
            <sec>-56</sec>
        </origin>
        <spacing>
            <x>112</x>
            <y>192</y>
            <z>576</z>
        </spacing>
        <cell>
            <a units="&#8491;">255.99936</a>
            <b units="&#8491;">148.00015</b>
            <c units="&#8491;">765.7977</c>
            <alpha units="deg">90.0</alpha>
            <beta units="deg">90.0</beta>
            <gamma units="deg">90.0</gamma>
        </cell>
        <axis_order>
            <fast>Z</fast>
            <medium>X</medium>
            <slow>Y</slow>
        </axis_order>
        <statistics>
            <minimum>-974.402832030000013</minimum>
            <maximum>977.198852539999962</maximum>
            <average>-0.00000001</average>
            <std>215.096801760000005</std>
        </statistics>
        <pixel_spacing>
            <x units="&#8491;">1.33333</x>
            <y units="&#8491;">1.32143</y>
            <z units="&#8491;">1.32951</z>
        </pixel_spacing>
        <contour_list>
            <contour primary="true">
                <level>430.0</level>
                <source>AUTHOR</source>
            </contour>
        </contour_list>
        <annotation_details>One unit cell of the acrosomal bundle, pseudo-centered to provide a orthogonal map from the pseudo-hexagonal packing</annotation_details>
        <details>::::EMDATABANK.org::::EMD-1088::::</details>
    </map>
    <interpretation>
        <modelling_list>
            <modelling>
                <initial_model>
                    <access_code>1ATN</access_code>
                </initial_model>
                <software_list>
                    <software>
                        <name>foldhunter and homemade software</name>
                    </software>
                </software_list>
                <details>Protocol: cross-correlation. each of the 28 actins was fitted and averaged, scruin was density-correlated and averaged because there is no crystal structure. overall B is the NEGATIVE B factor applied as a high-pass filter in the calculation of the map (-500).</details>
                <target_criteria>cross-correlation</target_criteria>
                <refinement_space>REAL</refinement_space>
                <overall_bvalue>-500.0</overall_bvalue>
            </modelling>
        </modelling_list>
    </interpretation>
</emd>