<?xml version="1.0" encoding="UTF-8"?>
<emd emdb_id="EMD-3127" version="3.0.1.9">
    <admin>
        <status_history_list>
            <status status_id="1">
                <code>REL</code>
            </status>
        </status_history_list>
        <current_status>
            <code>OBS</code>
            <processing_site>PDBe</processing_site>
        </current_status>
        <sites>
            <deposition>PDBe</deposition>
            <last_processing>PDBe</last_processing>
        </sites>
        <key_dates>
            <deposition>2015-08-13</deposition>
            <header_release>2015-09-16</header_release>
            <map_release>2017-02-01</map_release>
            <obsolete>2017-02-01</obsolete>
            <update>2017-02-01</update>
        </key_dates>
        <title>Structure of a cross-beta amyloid fibril from IGSNVVTWYQQL peptide of AL-DIA immunoglobulin light chain by cryo-EM and fiber diffraction</title>
        <authors_list>
            <author>Schmidt A</author>
            <author>Annamalai K</author>
            <author>Schmidt M</author>
            <author>Grigorieff N</author>
            <author>Fandrich M</author>
        </authors_list>
        <keywords>AL amyloidosis, cryo electron microscopy, steric zipper, three dimensional reconstruction</keywords>
    </admin>
    <crossreferences>
        <citation_list>
            <primary_citation>
                <journal_citation published="false">
                    <author order="1">Schmidt A</author>
                    <author order="2">Annamalai K</author>
                    <author order="3">Schmidt M</author>
                    <author order="4">Grigorieff N</author>
                    <author order="5">Fandrich M</author>
                    <title>Structural hierarchy, polymorphism and zipper-like packing of amyloid fibrils from an immunoglobulin light chain fragment</title>
                    <journal>To Be Published</journal>
                </journal_citation>
            </primary_citation>
        </citation_list>
    </crossreferences>
    <sample>
        <name>Amyloidogenic Fragment IGSNVVTWYQQL of Immunoglobulin Light Chain of Human AL Patient</name>
        <supramolecule_list>
            <sample_supramolecule supramolecule_id="1000">
                <name>Amyloidogenic Fragment IGSNVVTWYQQL of Immunoglobulin Light Chain of Human AL Patient</name>
                <details>The sample forms long amyloid-like fibrils.</details>
                <number_unique_components>1</number_unique_components>
            </sample_supramolecule>
        </supramolecule_list>
        <macromolecule_list>
            <protein_or_peptide macromolecule_id="1">
                <name>Immunoglobulin Light Chain</name>
                <natural_source database="NCBI">
                    <organism ncbi="9606">Homo sapiens</organism>
                    <synonym_organism>Human</synonym_organism>
                    <tissue>Blood</tissue>
                    <cell>Plasma cell</cell>
                    <cellular_location>extracellular</cellular_location>
                </natural_source>
                <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>filament</aggregation_state>
            <specimen_preparation_list>
                <helical_preparation preparation_id="1">
                    <concentration units="mg/mL">5.0</concentration>
                    <buffer>
                        <ph>8.0</ph>
                        <details>50mM Tris-HCL</details>
                    </buffer>
                    <grid>
                        <details>C-flat 1.2/1.3-2C 400 mesh grids,
glow discharged</details>
                    </grid>
                    <vitrification>
                        <cryogen_name>ETHANE</cryogen_name>
                        <chamber_humidity units="percentage">50</chamber_humidity>
                        <chamber_temperature units="K">100</chamber_temperature>
                        <instrument>GATAN CRYOPLUNGE 3</instrument>
                        <method>Incubation of 0.014 mg/ml fibril solution on glow discharged holey carbon grid for 30 seconds and backside blotting for 4 seconds before plunging.</method>
                    </vitrification>
                </helical_preparation>
            </specimen_preparation_list>
            <microscopy_list>
                <helical_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">2.0</nominal_cs>
                    <nominal_defocus_min units="µm">1.0</nominal_defocus_min>
                    <nominal_defocus_max units="µm">5.0</nominal_defocus_max>
                    <nominal_magnification>50000.0</nominal_magnification>
                    <calibrated_magnification>66350.69999999999709</calibrated_magnification>
                    <specimen_holder_model>GATAN LIQUID NITROGEN</specimen_holder_model>
                    <temperature>
                        <temperature_average units="K">100</temperature_average>
                    </temperature>
                    <date>2012-11-12</date>
                    <image_recording_list>
                        <image_recording>
                            <film_or_detector_model category="CCD">FEI FALCON I (4k x 4k)</film_or_detector_model>
                            <number_real_images>5</number_real_images>
                            <average_electron_dose_per_image units="e/Å^2">25</average_electron_dose_per_image>
                            <bits_per_pixel>16.0</bits_per_pixel>
                        </image_recording>
                    </image_recording_list>
                </helical_microscopy>
            </microscopy_list>
            <helical_processing image_processing_id="1">
                <final_reconstruction>
                    <applied_symmetry>
                        <helical_parameters>
                            <delta_z units="Å">4.69</delta_z>
                            <delta_phi units="deg">0.824</delta_phi>
                            <axial_symmetry>C2</axial_symmetry>
                        </helical_parameters>
                    </applied_symmetry>
                    <algorithm>OTHER</algorithm>
                    <resolution units="Å" res_type="BY AUTHOR">28.5</resolution>
                    <resolution_method>OTHER</resolution_method>
                    <software_list>
                        <software>
                            <name>Frealix</name>
                        </software>
                    </software_list>
                    <details>Final map was calculated from five single fibril reconstructions.</details>
                </final_reconstruction>
                <ctf_correction>
                    <details>Defocus estimated for each helical subunit</details>
                </ctf_correction>
            </helical_processing>
        </structure_determination>
    </structure_determination_list>
    <map format="CCP4" size_kbytes="142">
        <file>emd_3127.map.gz</file>
        <symmetry>
            <space_group>1</space_group>
        </symmetry>
        <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
        <dimensions>
            <col>30</col>
            <row>30</row>
            <sec>40</sec>
        </dimensions>
        <origin>
            <col>-15</col>
            <row>-15</row>
            <sec>-20</sec>
        </origin>
        <spacing>
            <x>30</x>
            <y>30</y>
            <z>40</z>
        </spacing>
        <cell>
            <a units="Å">253.19998</a>
            <b units="Å">253.19998</b>
            <c units="Å">337.59998</c>
            <alpha units="deg">90.0</alpha>
            <beta units="deg">90.0</beta>
            <gamma units="deg">90.0</gamma>
        </cell>
        <axis_order>
            <fast>X</fast>
            <medium>Y</medium>
            <slow>Z</slow>
        </axis_order>
        <statistics>
            <minimum>-2020.4296875</minimum>
            <maximum>8514.20019531</maximum>
            <average>695.82000732</average>
            <std>2629.44335938</std>
        </statistics>
        <pixel_spacing>
            <x units="Å">8.44</x>
            <y units="Å">8.44</y>
            <z units="Å">8.44</z>
        </pixel_spacing>
        <contour_list>
            <contour primary="true">
                <level>0.48</level>
                <source>AUTHOR</source>
            </contour>
        </contour_list>
        <annotation_details>Reconstruction morphology 2 of a left handed amyloid-like fibril of the IGSNVVTWYQQL fragment of an immunoglobulin light chain</annotation_details>
        <details>::::EMDATABANK.org::::EMD-3127::::</details>
    </map>
    <interpretation>
        <figure_list>
            <figure>
                <file>emd_3127.png</file>
            </figure>
        </figure_list>
    </interpretation>
    <validation>
        <fsc_curve>
            <file>emd_3127_fsc.xml</file>
        </fsc_curve>
    </validation>
</emd>
