Crystal structure and orientation of organic semiconductor thin films by microcrystal electron diffraction and grazing-incidence wide-angle X-ray scattering

Levine, A. M.; Bu, Guanhong; Biswas, Sankarsan; Tsai, Esther H. R.; Braunschweig, Adam B.; Nannenga, Brent L.

doi:10.1039/d0cc00119h

Cited by 26 publications

(26 citation statements)

References 28 publications

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“…We demonstrated cryoFIB milled lamella give higher resolution data of better quality when compared to nanocrystals under the same imaging conditions. We showed that the low cost Ceta-D camera, generally accessible in a standard cryoEM setup, worked well for microED for well diffracting samples, as reported recently by others ( Hattne et al, 2019 ; Martynowycz et al, 2019 ; Wang et al, 2019 ; Levine et al, 2020 ). We show a better structure (2.0 Å) than that reported for lamella of proteinase K using Ceta-D detector (2.75 Å) ( Martynowycz et al, 2019 ).…”

Section: Resultssupporting

confidence: 83%

A Workflow for Protein Structure Determination From Thin Crystal Lamella by Micro-Electron Diffraction

Beale

Waterman

Hecksel

et al. 2020

Front. Mol. Biosci.

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MicroED has recently emerged as a powerful method for the analysis of biological structures at atomic resolution. This technique has been largely limited to protein nanocrystals which grow either as needles or plates measuring only a few hundred nanometers in thickness. Furthermore, traditional microED data processing uses established X-ray crystallography software that is not optimized for handling compound effects that are unique to electron diffraction data. Here, we present an integrated workflow for microED, from sample preparation by cryo-focused ion beam milling, through data collection with a standard Ceta-D detector, to data processing using the DIALS software suite, thus enabling routine atomic structure determination of protein crystals of any size and shape using microED. We demonstrate the effectiveness of the workflow by determining the structure of proteinase K to 2.0 Å resolution and show the advantage of using protein crystal lamellae over nanocrystals.

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Section: Resultssupporting

confidence: 83%

A Workflow for Protein Structure Determination From Thin Crystal Lamella by Micro-Electron Diffraction

Beale

Waterman

Hecksel

et al. 2020

Front. Mol. Biosci.

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“…In order to further characterize the isolated compound, we used MicroED for high-resolution structure determination. There are several methods for preparing small molecule samples for the TEM, including applying powdered sample directly to the grid, applying a crystalline suspension to the grid followed by drying, and direct crystal growth on the grid by solvent evaporation (van Genderen et al, 2016;Gruene et al, 2018;Jones et al, 2018;Banihashemi et al, 2020;Levine et al, 2020). For this analysis, preparing the EM grids with the sample was performed by simply placing the grids in a small amount of material as described above, a process which took less than 1 min.…”

Section: Resultsmentioning

confidence: 99%

“…Furthermore, the recent development of techniques such as microcrystal electron diffraction (MicroED) have enabled the determination of the structures of both large biomolecules and small molecules in crystalline form (Gemmi et al, 2019;Nannenga and Gonen, 2019;Nannenga, 2020). Electron diffraction has been successfully applied to a wide variety of samples including proteins, peptides, small organic molecules, and inorganic materials (Mugnaioli et al, 2009(Mugnaioli et al, , 2012(Mugnaioli et al, , 2018Zhang et al, 2013Zhang et al, , 2018Nannenga et al, 2014a,b;Rodriguez et al, 2015;Simancas et al, 2016;van Genderen et al, 2016;Clabbers et al, 2017Clabbers et al, , 2020Krotee et al, 2017;Palatinus et al, 2017;Rozhdestvenskaya et al, 2017;Das et al, 2018;Gallagher-Jones et al, 2018;Gruene et al, 2018;Hughes et al, 2018;Jones et al, 2018;Liu and Gonen, 2018;Seidler et al, 2018;Brázda et al, 2019;Dick et al, 2019;Lanza et al, 2019;Warmack et al, 2019;Wennmacher et al, 2019;Xu et al, 2019;Zatsepin et al, 2019;Banihashemi et al, 2020;Levine et al, 2020;Zhu et al, 2020). A major benefit to this technique is that the micro and nanocrystals used for MicroED are several orders of magnitude smaller than those used in conventional X-ray crystallography.…”

Section: Introductionmentioning

confidence: 99%

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Rapid Structural Analysis of a Synthetic Non-canonical Amino Acid by Microcrystal Electron Diffraction

Gleason

Nannenga

Mills

2021

Front. Mol. Biosci.

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Structural characterization of small molecules is a crucial component of organic synthesis. In this work, we applied microcrystal electron diffraction (MicroED) to analyze the structure of the product of an enzymatic reaction that was intended to produce the unnatural amino acid 2,4-dihydroxyphenylalanine (24DHF). Characterization of our isolated product with nuclear magnetic resonance spectroscopy (NMR) and mass spectrometry (MS) suggested that an isomer of 24DHF had been formed. Microcrystals present in the isolated product were then used to determine its structure to 0.62 Å resolution, which confirmed its identity as 2-amino-2-(2,4-dihydroxyphenyl)propanoic acid (24DHPA). Moreover, the MicroED structural model indicated that both enantiomeric forms of 24DHPA were present in the asymmetric unit. Notably, the entire structure determination process including setup, data collection, and refinement was completed in ~1 h. The MicroED data not only bolstered previous results obtained using NMR and MS but also immediately provided information about the stereoisomers present in the product, which is difficult to achieve using NMR and MS alone. Our results therefore demonstrate that MicroED methods can provide useful structural information on timescales that are similar to many commonly used analytical methods and can be added to the existing suite of small molecule structure determination tools in future studies.

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“…[9a] Microcrystal electron diffraction (MicroED) has recently emerged as aw ay to circumvent limitations related to crystal growth since it can allow highresolution structural data to be acquired on nanocrystalline samples. [10] In this contribution, we use ac ombination of divergent synthesis and MicroED to interrogate solid-state behavior in an ew family of expanded helicenes.T he quinone-and quinoxiline-containing helicenes 2-mon, 2-di, 3-mon,and 3-di (Scheme 1b)w ere targeted due to their electron deficiency, which tends to promote strong intermolecular interactions between p-systems. [8a,11] Then ew compounds were accessed via ah ighly selective oxidative dearomatization of electronrich 1a,w hich provided derivatives of the same or reduced symmetry.W hile uncontrollable crystallization kinetics consistently resulted in the formation of microcrystals that were unsuitable for single crystal X-ray diffraction, the application of MicroED enabled the rapid acquisition of high resolution data for all five helicenes.T his data revealed three different packing motifs,r epresenting four different space groups.…”

Section: Introductionmentioning

confidence: 99%

Elucidation of Diverse Solid‐State Packing in a Family of Electron‐Deficient Expanded Helicenes via Microcrystal Electron Diffraction (MicroED)**

et al. 2020

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Solid-state packing plays a defining role in the properties of a molecular organic material, but it is difficult to elucidate in the absence of single crystals that are suitable for X-ray diffraction. Here, we demonstrate the coupling of divergent synthesis with microcrystal electron diffraction (MicroED) for rapid assessment of solid-state packing motifs, using a class of chiral nanocarbonsexpanded helicenesas a proof of concept. Two highly selective oxidative dearomatizations of a readily-accessible helicene provided a divergent route to four electron-deficient analogues containing quinone or quinoxaline units. Crystallization efforts consistently yielded microcrystals that were unsuitable for single crystal X-ray diffraction, but ideal for MicroED. This technique facilitated the elucidation of solid-state structures of all five compounds with <1.1 Å resolution. The otherwise-inaccessible data revealed a range of notable packing behavior, including four different space groups, homochirality in a crystal for a helicene with an extremely low enantiomerization barrier, and nanometer scale cavities. The results of this study suggest that MicroED will soon become an indispensable tool for high-throughput investigations in pursuit of next-generation organic materials. 4 Figure 3. Solid-state MicroED structures of (a) 1a, (b) 2-di, (c) 2-mon, (d) 3-mon, and (e) 3-di. *The starred distances represent helical pitch values for the associated helicene, which were estimated as described in Figure 4. † The crystals of 2-di feature helicenes with two different pitch values.

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Crystal structure and orientation of organic semiconductor thin films by microcrystal electron diffraction and grazing-incidence wide-angle X-ray scattering

Abstract: The complementary methods of MicroED and GIWAXS provide insight into crystal structure arrangement in organic semiconductor thin films.

Cited by 26 publications

References 28 publications

A Workflow for Protein Structure Determination From Thin Crystal Lamella by Micro-Electron Diffraction

A Workflow for Protein Structure Determination From Thin Crystal Lamella by Micro-Electron Diffraction

Rapid Structural Analysis of a Synthetic Non-canonical Amino Acid by Microcrystal Electron Diffraction

Elucidation of Diverse Solid‐State Packing in a Family of Electron‐Deficient Expanded Helicenes via Microcrystal Electron Diffraction (MicroED)**

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