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Machining protein microcrystals for structure determination by electron diffraction.
Duyvesteyn, Helen M E; Kotecha, Abhay; Ginn, Helen M; Hecksel, Corey W; Beale, Emma V; de Haas, Felix; Evans, Gwyndaf; Zhang, Peijun; Chiu, Wah; Stuart, David I.
Affiliation
  • Duyvesteyn HME; Division of Structural Biology, University of Oxford, Headington, Oxford OX3 7BN, United Kingdom.
  • Kotecha A; Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, United Kingdom.
  • Ginn HM; Division of Structural Biology, University of Oxford, Headington, Oxford OX3 7BN, United Kingdom.
  • Hecksel CW; Materials and Structural Analysis, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 GG, Eindhoven, The Netherlands.
  • Beale EV; Division of Structural Biology, University of Oxford, Headington, Oxford OX3 7BN, United Kingdom.
  • de Haas F; Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, United Kingdom.
  • Evans G; Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, United Kingdom.
  • Zhang P; Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, United Kingdom.
  • Chiu W; Materials and Structural Analysis, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 GG, Eindhoven, The Netherlands.
  • Stuart DI; Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, United Kingdom.
Proc Natl Acad Sci U S A ; 115(38): 9569-9573, 2018 09 18.
Article in En | MEDLINE | ID: mdl-30171169
ABSTRACT
We demonstrate that ion-beam milling of frozen, hydrated protein crystals to thin lamella preserves the crystal lattice to near-atomic resolution. This provides a vehicle for protein structure determination, bridging the crystal size gap between the nanometer scale of conventional electron diffraction and micron scale of synchrotron microfocus beamlines. The demonstration that atomic information can be retained suggests that milling could provide such detail on sections cut from vitrified cells.
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Full text: 1 Database: MEDLINE Main subject: Muramidase / Crystallography, X-Ray / Microtechnology Language: En Year: 2018 Type: Article

Full text: 1 Database: MEDLINE Main subject: Muramidase / Crystallography, X-Ray / Microtechnology Language: En Year: 2018 Type: Article