Data

Derivatives for structure solution of the peripheral stalk from T.thermophilus A-ATPase

Monash University
Australian Synchrotron (Associated with)
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ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=https://store.synchrotron.org.au/experiment/view/210/#metadata&rft.title=Derivatives for structure solution of the peripheral stalk from T.thermophilus A-ATPase&rft.identifier=https://store.synchrotron.org.au/experiment/view/210/#metadata&rft.publisher=Monash University&rft.description=Rotary ATPases couple ATP hydrolysis/synthesis with proton translocation across biological membranes and so are central components of the biological energy conversion machinery. Their peripheral stalks are essential components that counteract torque generated by rotation of the central stalk during ATP synthesis or hydrolysis.These datasets are derivatives of the peripheral stalk from T.thermophilus A-ATPase. Native crystals were soaked in Lutetium(III) acetate (2K7c_3_###.img) and Dysprosium(III) chloride (2K3#######.img).Resulting maps were used to create the pdb model 3V6I. The model was used to identify bending and twisting motions inherent within the structure that accommodate movements within the ATPase.   Beamline: MX2 EPN: 3511 PDB: 3V61 Organism: Thermus thermophilus HB8   Expression System: Escherichia coli Sequence: >3V6I:B|PDBID|CHAIN|SEQUENCE GMGGLGLIKSLAEKEKQLLERLEAAKKEAEERVKRAEAEAKALLEEAEAKAKALEAQYRERERAETEALLARYRERAEAE AKAVREKAMARLDEAVALVLKEVLP   &rft.creator=Anonymous&rft.date=2014&rft.relation=http://www.ncbi.nlm.nih.gov/pubmed/22353718&rft_rights=This experiment data is licensed under Creative Commons Attribution 3.0 Australia (CC BY 3.0). http://creativecommons.org/licenses/by/3.0/au/&rft_subject=OTHER BIOLOGICAL SCIENCES&rft_subject=BIOLOGICAL SCIENCES&rft_subject=Synchrotrons; Accelerators; Instruments and Techniques&rft_subject=PHYSICAL SCIENCES&rft_subject=OTHER PHYSICAL SCIENCES&rft_subject=Thermus thermophilus&rft_subject=Escherichia coli&rft_subject=Macromolecular Crystallography&rft_subject=MX2&rft.type=dataset&rft.language=English Access the data
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This experiment data is licensed under Creative Commons Attribution 3.0 Australia (CC BY 3.0).
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Rotary ATPases couple ATP hydrolysis/synthesis with proton translocation across biological membranes and so are central components of the biological energy conversion machinery. Their peripheral stalks are essential components that counteract torque generated by rotation of the central stalk during ATP synthesis or hydrolysis.

These datasets are derivatives of the peripheral stalk from T.thermophilus A-ATPase. Native crystals were soaked in Lutetium(III) acetate (2K7c_3_###.img) and Dysprosium(III) chloride (2K3#######.img).

Resulting maps were used to create the pdb model 3V6I. The model was used to identify bending and twisting motions inherent within the structure that accommodate movements within the ATPase.

 

  • Beamline: MX2
  • EPN: 3511
  • PDB: 3V61
  • Organism: Thermus thermophilus HB8  
  • Expression System: Escherichia coli
  • Sequence: >3V6I:B|PDBID|CHAIN|SEQUENCE GMGGLGLIKSLAEKEKQLLERLEAAKKEAEERVKRAEAEAKALLEEAEAKAKALEAQYRERERAETEALLARYRERAEAE AKAVREKAMARLDEAVALVLKEVLP  

Available: 24 03 2014

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Subjects
Biological Sciences | Escherichia coli | MX2 | Macromolecular Crystallography | Other Biological Sciences | Other Physical Sciences | Physical Sciences | Synchrotrons; Accelerators; Instruments and Techniques | Thermus thermophilus |

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