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        <current_status>
            <date>2024-11-06</date>
            <code>REL</code>
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            <last_processing>PDBj</last_processing>
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        <key_dates>
            <deposition>2019-11-13</deposition>
            <header_release>2019-12-04</header_release>
            <map_release>2019-12-04</map_release>
            <update>2024-11-06</update>
        </key_dates>
        <grant_support>
            <grant_reference>
                <funding_body>National Natural Science Foundation of China</funding_body>
                <code>31570730</code>
                <country>China</country>
            </grant_reference>
            <grant_reference>
                <funding_body>National Natural Science Foundation of China</funding_body>
                <code>31722015</code>
                <country>China</country>
            </grant_reference>
            <grant_reference>
                <funding_body>Ministry of Science and Technology (China)</funding_body>
                <code>2016YFA0501102</code>
                <country>China</country>
            </grant_reference>
            <grant_reference>
                <funding_body>Ministry of Science and Technology (China)</funding_body>
                <code>2016YFA0501902</code>
                <country>China</country>
            </grant_reference>
        </grant_support>
        <title>MicroED structure of proteinase K at 1.50A determained using crystal lamellas prepared by focused ion beam milling</title>
        <authors_list>
            <author>Zhou H</author>
            <author>Luo Z</author>
        </authors_list>
        <keywords>Proteinase K, MicroED, Focused Ion Beam, crystal lamella, HYDROLASE</keywords>
    </admin>
    <crossreferences>
        <citation_list>
            <primary_citation>
                <journal_citation published="true">
                    <author order="1">Zhou H</author>
                    <author order="2">Luo Z</author>
                    <author order="3">Li X</author>
                    <title>Using focus ion beam to prepare crystal lamella for electron diffraction.</title>
                    <journal_abbreviation>J. Struct. Biol.</journal_abbreviation>
                    <country>US</country>
                    <volume>205</volume>
                    <first_page>59</first_page>
                    <last_page>64</last_page>
                    <year>2019</year>
                    <external_references type="PUBMED">30794865</external_references>
                    <external_references type="DOI">doi:10.1016/j.jsb.2019.02.004</external_references>
                    <external_references type="ISSN">1095-8657</external_references>
                    <external_references type="CSD">0803</external_references>
                    <external_references type="ASTM">JSBIEM</external_references>
                </journal_citation>
            </primary_citation>
        </citation_list>
        <pdb_list>
            <pdb_reference>
                <pdb_id>6law</pdb_id>
                <relationship>
                    <in_frame>FULLOVERLAP</in_frame>
                </relationship>
            </pdb_reference>
        </pdb_list>
    </crossreferences>
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        <name>proteinase K</name>
        <supramolecule_list>
            <complex_supramolecule supramolecule_id="1">
                <name>proteinase K</name>
                <parent>0</parent>
                <macromolecule_list>
                    <macromolecule>
                        <macromolecule_id>1</macromolecule_id>
                    </macromolecule>
                </macromolecule_list>
                <natural_source database="NCBI">
                    <organism ncbi="37998">Parengyodontium album</organism>
                </natural_source>
            </complex_supramolecule>
        </supramolecule_list>
        <macromolecule_list>
            <protein_or_peptide macromolecule_id="1">
                <name>Proteinase K</name>
                <natural_source database="NCBI">
                    <organism ncbi="37998">Parengyodontium album</organism>
                </natural_source>
                <molecular_weight>
                    <theoretical units="MDa">0.028958791</theoretical>
                </molecular_weight>
                <number_of_copies>1</number_of_copies>
                <enantiomer>LEVO</enantiomer>
                <sequence>
                    <string>AAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFEGRAQMVKTYYYSSRDGNGHGTHCAGTVGSR
TYGVAKKTQLFGVKVLDDNGSGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQSSGVMVAVAAG
NNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLDIFGPGTDILSTWIGGSTRSISGTSMATPHVAGLAAYLMTL
GKTTAASACRYIADTANKGDLSNIPFGTVNLLAYNNYQA</string>
                    <external_references type="UNIPROTKB">P06873</external_references>
                </sequence>
                <ec_number>3.4.21.64</ec_number>
            </protein_or_peptide>
            <ligand macromolecule_id="2">
                <name>SULFATE ION</name>
                <molecular_weight>
                    <theoretical units="MDa">9.606299999999999e-05</theoretical>
                </molecular_weight>
                <number_of_copies>1</number_of_copies>
                <formula>SO4</formula>
            </ligand>
            <ligand macromolecule_id="3">
                <name>water</name>
                <molecular_weight>
                    <theoretical units="MDa">1.8015e-05</theoretical>
                </molecular_weight>
                <number_of_copies>230</number_of_copies>
                <formula>HOH</formula>
            </ligand>
        </macromolecule_list>
    </sample>
    <structure_determination_list>
        <structure_determination structure_determination_id="1">
            <method>electronCrystallography</method>
            <aggregation_state>threeDArray</aggregation_state>
            <specimen_preparation_list>
                <crystallography_preparation preparation_id="1">
                    <buffer>
                        <ph>7.5</ph>
                    </buffer>
                    <vitrification>
                        <cryogen_name>ETHANE</cryogen_name>
                    </vitrification>
                </crystallography_preparation>
            </specimen_preparation_list>
            <microscopy_list>
                <crystallography_microscopy microscopy_id="1">
                    <microscope>FEI TECNAI F20</microscope>
                    <illumination_mode>FLOOD BEAM</illumination_mode>
                    <imaging_mode>DIFFRACTION</imaging_mode>
                    <electron_source>FIELD EMISSION GUN</electron_source>
                    <acceleration_voltage units="kV">200</acceleration_voltage>
                    <image_recording_list>
                        <image_recording image_recording_id="1">
                            <film_or_detector_model>GATAN ULTRASCAN 4000 (4k x 4k)</film_or_detector_model>
                            <average_electron_dose_per_image units="e/Å^2">0.028</average_electron_dose_per_image>
                        </image_recording>
                    </image_recording_list>
                    <camera_length units="mm">1000</camera_length>
                </crystallography_microscopy>
            </microscopy_list>
            <crystallography_processing image_processing_id="1">
                <image_recording_id>1</image_recording_id>
                <final_reconstruction>
                    <resolution units="Å" res_type="BY AUTHOR">1.5</resolution>
                    <resolution_method>DIFFRACTION PATTERN/LAYERLINES</resolution_method>
                </final_reconstruction>
                <crystallography_statistics>
                    <number_intensities_measured>200471</number_intensities_measured>
                    <number_structure_factors>37742</number_structure_factors>
                    <fourier_space_coverage>91.099999999999994</fourier_space_coverage>
                    <r_sym>0.245</r_sym>
                    <r_merge>0.245</r_merge>
                    <overall_phase_error>0</overall_phase_error>
                    <overall_phase_residual>1.0</overall_phase_residual>
                    <phase_error_rejection_criteria>60</phase_error_rejection_criteria>
                    <high_resolution units="Å">1.5</high_resolution>
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                        <shell shell_id="1">
                            <high_resolution units="Å">1.5</high_resolution>
                            <low_resolution units="Å">1.55</low_resolution>
                            <number_structure_factors>3693</number_structure_factors>
                            <phase_residual>1.0</phase_residual>
                            <fourier_space_coverage>90.599999999999994</fourier_space_coverage>
                            <multiplicity>5.2</multiplicity>
                        </shell>
                    </shell_list>
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            <a units="Å">69.313995</a>
            <b units="Å">69.313995</b>
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            <alpha units="deg">90.0</alpha>
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    <interpretation>
        <modelling_list>
            <modelling>
                <refinement_protocol>FLEXIBLE FIT</refinement_protocol>
                <refinement_space>RECIPROCAL</refinement_space>
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