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        <sites>
            <deposition>PDBe</deposition>
            <last_processing>PDBe</last_processing>
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        <key_dates>
            <deposition>2002-06-18</deposition>
            <header_release>2002-06-20</header_release>
            <map_release>2002-06-20</map_release>
            <update>2012-12-26</update>
        </key_dates>
        <title>Real space refinement of acto-myosin structures from sectioned muscle.</title>
        <authors_list>
            <author>Chen LF</author>
            <author>Blanc E</author>
            <author>Chapman MS</author>
            <author>Taylor KA</author>
        </authors_list>
        <keywords />
    </admin>
    <crossreferences>
        <citation_list>
            <primary_citation>
                <journal_citation published="true">
                    <author order="1">Chen LF</author>
                    <author order="2">Blanc E</author>
                    <author order="3">Chapman MS</author>
                    <author order="4">Taylor KA</author>
                    <title>Real space refinement of acto-myosin structures from sectioned muscle.</title>
                    <journal>J.STRUCT.BIOL.</journal>
                    <volume>133</volume>
                    <first_page>221</first_page>
                    <last_page>232</last_page>
                    <year>2001</year>
                    <external_references type="PUBMED">11472093</external_references>
                    <external_references type="DOI">doi:10.1006/jsbi.2000.4321</external_references>
                </journal_citation>
            </primary_citation>
        </citation_list>
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    <sample>
        <name>Rigor insect flight muscle from Lethocerus maximus</name>
        <supramolecule_list>
            <sample_supramolecule supramolecule_id="1000">
                <name>Rigor insect flight muscle from Lethocerus maximus</name>
                <details>The sample is a single filament layer cut from myofibrils by ultramicrotomy. The section thickness is ~25 nm. Specimen has been chemically fixed, dehydrated, embedded in Araldite and sectioned with a diamond knife.</details>
                <oligomeric_state>Thick myosin containing filament and thin actin-containing filaments.</oligomeric_state>
                <number_unique_components>2</number_unique_components>
            </sample_supramolecule>
            <organelle_or_cellular_component_supramolecule supramolecule_id="1">
                <name synonym="myosin">thick, myosin-containing filament</name>
                <details>Filaments contain more than just myosin</details>
                <recombinant_exp_flag>false</recombinant_exp_flag>
                <natural_source database="NCBI">
                    <organism ncbi="43338">Lethocerus</organism>
                    <synonym_organism>water bug, Lethocerus maximus</synonym_organism>
                    <tissue>Indirect flight muscles</tissue>
                    <cell>muscle fibers</cell>
                    <organelle>myofibrils</organelle>
                    <cellular_location>myofibrils</cellular_location>
                </natural_source>
                <recombinant_expression database="NCBI" />
            </organelle_or_cellular_component_supramolecule>
            <organelle_or_cellular_component_supramolecule supramolecule_id="2">
                <name synonym="actin">thin, actin-containing filament</name>
                <details>filaments contain more than just actin</details>
                <oligomeric_state>polar, 2-stranded helical filament, helical symmetry is 28/13</oligomeric_state>
                <recombinant_exp_flag>false</recombinant_exp_flag>
                <natural_source database="NCBI">
                    <organism ncbi="43338">Lethocerus</organism>
                    <synonym_organism>water bug, Lethocerus maximus</synonym_organism>
                    <tissue>Indirect flight muscles</tissue>
                    <cell>Muscle fibers</cell>
                    <organelle>myofibrils</organelle>
                    <cellular_location>myofibrils</cellular_location>
                </natural_source>
                <recombinant_expression database="NCBI" />
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            <method>tomography</method>
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                    <vitrification>
                        <cryogen_name>NONE</cryogen_name>
                    </vitrification>
                </tomography_preparation>
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                <tomography_microscopy microscopy_id="1">
                    <microscope>FEI/PHILIPS EM400</microscope>
                    <illumination_mode>FLOOD BEAM</illumination_mode>
                    <imaging_mode>BRIGHT FIELD</imaging_mode>
                    <electron_source>TUNGSTEN HAIRPIN</electron_source>
                    <acceleration_voltage units="kV">100</acceleration_voltage>
                    <nominal_magnification>17000.0</nominal_magnification>
                    <specimen_holder_model>PHILIPS ROTATION HOLDER</specimen_holder_model>
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                        <temperature_min units="K">25</temperature_min>
                        <temperature_max units="K">25</temperature_max>
                        <temperature_average units="K">25</temperature_average>
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                            <number_real_images>24</number_real_images>
                            <bits_per_pixel>16.</bits_per_pixel>
                        </image_recording>
                    </image_recording_list>
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                            <max_angle units="deg">59.4</max_angle>
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                <details>Double axis tilt series collected on film. Digitized on
          PDS       1010M densitometer. Other relevent references K. A.
          Taylor, M. C.       Reedy, L. Cordova and M. K. Reedy. 3-D
          structure of insect flight       muscle in rigor from tilted
          thin sections. Nature 310, 28 5-291       (1984). Hanspeter
          Winkler and Kenneth A. Taylor. Multivariate       statistical
          analysis of three-dimensional cross-bridge motifs in
          insect flight muscle. Ultramicroscopy 77, 141-152 (1999).
          Chen, Li       Fan, Winkler, Hanspeter, Reedy, Michael K., Ree
          dy, Mary C. and       Taylor, Kenneth A.. Molecular Modeling
          of Averaged Rigor       Crossbridges from Tomograms of Insect
          Flight Muscle. J. Struct.       Biol. 138(2), 92-104 (2002)</details>
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        the       tilt series using crosscorrelation functions, such as
        phase only       and the VanHeel Mutual Correlation Function.
        The sampling in each       micrographof a tilted specimen was
        match by interpolation to th e       lower angle members of the
        tilt series. This matching of areas and       sampling was done
        by a 4 parameter grid search. Once aligned and       scaled, the
        data were combined in Fourier space using a
        Whittaker-Shannon interpolation scheme. The map was calculated
        using a reverse Fourier transformation. The software used for
        the       reconstruction was in-house and adapted from in some
        cases from       MRC software.</details>
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                    <details>none</details>
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