4 research outputs found
Nanoscale mosaicity revealed in peptide microcrystals by scanning electron nanodiffraction.
Changes in lattice structure across sub-regions of protein crystals are challenging to assess when relying on whole crystal measurements. Because of this difficulty, macromolecular structure determination from protein micro and nanocrystals requires assumptions of bulk crystallinity and domain block substructure. Here we map lattice structure across micron size areas of cryogenically preserved three-dimensional peptide crystals using a nano-focused electron beam. This approach produces diffraction from as few as 1500 molecules in a crystal, is sensitive to crystal thickness and three-dimensional lattice orientation. Real-space maps reconstructed from unsupervised classification of diffraction patterns across a crystal reveal regions of crystal order/disorder and three-dimensional lattice tilts on the sub-100nm scale. The nanoscale lattice reorientation observed in the micron-sized peptide crystal lattices studied here provides a direct view of their plasticity. Knowledge of these features facilitates an improved understanding of peptide assemblies that could aid in the determination of structures from nano- and microcrystals by single or serial crystal electron diffraction
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Nanoscale mosaicity revealed in peptide microcrystals by scanning electron nanodiffraction.
Changes in lattice structure across sub-regions of protein crystals are challenging to assess when relying on whole crystal measurements. Because of this difficulty, macromolecular structure determination from protein micro and nanocrystals requires assumptions of bulk crystallinity and domain block substructure. Here we map lattice structure across micron size areas of cryogenically preserved three-dimensional peptide crystals using a nano-focused electron beam. This approach produces diffraction from as few as 1500 molecules in a crystal, is sensitive to crystal thickness and three-dimensional lattice orientation. Real-space maps reconstructed from unsupervised classification of diffraction patterns across a crystal reveal regions of crystal order/disorder and three-dimensional lattice tilts on the sub-100nm scale. The nanoscale lattice reorientation observed in the micron-sized peptide crystal lattices studied here provides a direct view of their plasticity. Knowledge of these features facilitates an improved understanding of peptide assemblies that could aid in the determination of structures from nano- and microcrystals by single or serial crystal electron diffraction
Recommended from our members
Nanoscale mosaicity revealed in peptide microcrystals by scanning electron nanodiffraction.
Changes in lattice structure across sub-regions of protein crystals are challenging to assess when relying on whole crystal measurements. Because of this difficulty, macromolecular structure determination from protein micro and nanocrystals requires assumptions of bulk crystallinity and domain block substructure. Here we map lattice structure across micron size areas of cryogenically preserved three-dimensional peptide crystals using a nano-focused electron beam. This approach produces diffraction from as few as 1500 molecules in a crystal, is sensitive to crystal thickness and three-dimensional lattice orientation. Real-space maps reconstructed from unsupervised classification of diffraction patterns across a crystal reveal regions of crystal order/disorder and three-dimensional lattice tilts on the sub-100nm scale. The nanoscale lattice reorientation observed in the micron-sized peptide crystal lattices studied here provides a direct view of their plasticity. Knowledge of these features facilitates an improved understanding of peptide assemblies that could aid in the determination of structures from nano- and microcrystals by single or serial crystal electron diffraction
Lattice nano-ripples revealed in peptide microcrystals by scanning electron nanodiffraction
Changes in lattice structure across sub-regions of protein crystals are
challenging to assess when relying on whole crystal measurements. Because of
this difficulty, macromolecular structure determination from protein micro and
nano crystals requires assumptions of bulk crystallinity and domain block
substructure. To evaluate the fidelity of these assumptions in protein
nanocrystals we map lattice structure across micron size areas of cryogenically
preserved three-dimensional peptide crystals using a nano-focused electron
beam. This approach produces diffraction from as few as 1,500 molecules in a
crystal, is sensitive to crystal thickness and three-dimensional lattice
orientation. Real-space maps reconstructed from unsupervised classification of
diffraction patterns across a crystal reveal regions of crystal order/disorder
and three-dimensional lattice reorientation on a 20nm scale. The lattice
nano-ripples observed in micron-sized macromolecular crystals provide a direct
view of their plasticity. Knowledge of these features is a first step to
understanding crystalline macromolecular self-assembly and improving the
determination of structures from protein nano and microcrystals from single or
serial crystal diffraction