Automated electron diffraction tomography – a new tool for nano crystal structure analysis

Kolb, Ute; Mugnaioli, Enrico; Gorelik, Tatiana E.

doi:10.1002/crat.201100036

Cited by 190 publications

(219 citation statements)

References 57 publications

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“…We plan to mount the detector on a Titan Krios machine, so data collection will be improved owing to the presence of an autoloader, a programmable goniometer and a programmable beam blanker. For small-molecule crystals, it has been reported that the collection of data in STEM diffraction mode further reduces beam damage (Kolb et al, 2011), so we plan to incorporate the Medipix2 detector in a microscope that has this option.…”

Section: Discussionmentioning

confidence: 99%

A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals

Nederlof

Genderen

et al. 2013

Acta Crystallogr D Biol Crystallogr

172

183

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When protein crystals are submicrometre-sized, X-ray radiation damage precludes conventional diffraction data collection. For crystals that are of the order of 100 nm in size, at best only single-shot diffraction patterns can be collected and rotation data collection has not been possible, irrespective of the diffraction technique used. Here, it is shown that at a very low electron dose (at most 0.1 e À Å À2 ), a Medipix2 quantum area detector is sufficiently sensitive to allow the collection of a 30-frame rotation series of 200 keV electrondiffraction data from a single $100 nm thick protein crystal. A highly parallel 200 keV electron beam ( = 0.025 Å ) allowed observation of the curvature of the Ewald sphere at low resolution, indicating a combined mosaic spread/beam divergence of at most 0.4 . This result shows that volumes of crystal with low mosaicity can be pinpointed in electron diffraction. It is also shown that strategies and data-analysis software (MOSFLM and SCALA) from X-ray protein crystallography can be used in principle for analysing electron-diffraction data from three-dimensional nanocrystals of proteins.

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Section: Discussionmentioning

confidence: 99%

A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals

Nederlof

Genderen

et al. 2013

Acta Crystallogr D Biol Crystallogr

172

183

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“…However, in the subsequent least-squares refinement, the dynamical diffraction effects, unavoidable in electron diffraction, have been mostly neglected and the data were treated as being kinematical. Despite attempts to limit the departure of the electron diffraction data from the kinematical limiteither by integrating the diffracted intensities using precession electron diffraction (PED; Vincent & Midgley, 1994;Mugnaioli et al, 2009), or by fine-slicing the diffraction spots as in the rotation electron diffraction (RED) method (Zhang et al, 2010), the refinements using this approximation yield high figures of merit and questionable accuracy of the refined structure parameters (Kolb et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Structure refinement using precession electron diffraction tomography and dynamical diffraction: tests on experimental data

Palatinus

Corrêa

Steciuk

et al. 2015

Acta Crystallogr B Struct Sci Cryst Eng Mater

134

137

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The recently published method for the structure refinement from threedimensional precession electron diffraction data using dynamical diffraction theory [Palatinus et al. (2015). Acta Cryst. A71, 235-244] has been applied to a set of experimental data sets from five different samples -Ni 2 Si, PrVO 3 , kaolinite, orthopyroxene and mayenite. The data were measured on different instruments and with variable precession angles. For each sample a reliable reference structure was available. A large series of tests revealed that the method provides structure models with an average error in atomic positions typically between 0.01 and 0.02 Å . The obtained structure models are significantly more accurate than models obtained by refinement using kinematical approximation for the calculation of model intensities. The method also allows a reliable determination of site occupancies and determination of absolute structure. Based on the extensive tests, an optimal set of the parameters for the method is proposed.

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“…Until quite recently, electron diffraction data collection was limited to sets of isolated 2-dimensional patterns that had to be merged with one another to form an incomplete set of 3-dimensional data. Efforts to devise a more automated and complete data collection strategy are now quite advanced [2,3], so this limitation can be expected to be reduced in future. Although electron diffraction intensities are distorted by a number of effects that are not easy to control or correct for, electron crystallography has been applied successfully to various classes of materials [4,5].…”

Section: Introductionmentioning

confidence: 99%

Electron crystallography as a complement to X-ray powder diffraction techniques

McCusker¹,

Baerlocher²

2013

Zeitschrift für Kristallographie - Crystalline Materials

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Abstract. Electron microscopy techniques yield information for crystal structure analysis that is remarkably complementary to that obtained from X-ray powder diffraction data. Structures of polycrystalline materials that resist solution by either method alone can sometimes be solved by combining the two. For example, the intensities extracted from an X-ray powder diffraction pattern are kinematical and can be interpreted easily, while those obtained from a typical selected area electron diffraction (SAED) or precession electron diffraction (PED) pattern are at least partially dynamical and therefore more difficult to use directly. On the other hand, many reflections in a powder diffraction pattern overlap and only the sum of their intensities can be measured, while those in an electron diffraction pattern are from a single crystal and therefore well separated in space. Although the intensities obtained from either SAED or PED data are less reliable than those obtained with Xrays, they can be used to advantage to improve the initial partitioning of the intensities of overlapping reflections. However, it is the partial crystallographic phase information that can be extracted either from high-resolution transmission electron microscopy (HRTEM) images or from PED data that has proven to be particularly useful in combination with high-resolution X-ray powder diffraction data. The dual-space (reciprocal and real space) structure determination programs Focus and Superflip have been shown to be especially useful for combining the two different types of data.

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Automated electron diffraction tomography – a new tool for nano crystal structure analysis

Cited by 190 publications

References 57 publications

A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals

A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals

Structure refinement using precession electron diffraction tomography and dynamical diffraction: tests on experimental data

Electron crystallography as a complement to X-ray powder diffraction techniques

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