Review: Electron Crystallography: Present Excitement, a Nod to the Past, Anticipating the Future

Glaeser, Robert M.

doi:10.1006/jsbi.1999.4172

Cited by 139 publications

(95 citation statements)

References 70 publications

(96 reference statements)

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“…Moreover, because UEM has been designed using femtosecond pulse trains from the oscillator alone, without the need for an ultrafast pulse amplifier, it has the added technological advantage of being beguilingly simple and easy to integrate. It may also prove unique (3) for limiting heat and blurring of images, and possibly radiation damage (9,81), points under study in this laboratory. Currently, we have one complete system operating at 120 keV, and shortly there will be three 4D UEMs, including single-pulse recordings at a higher number of electrons but with picosecond resolution.…”

Section: Discussionmentioning

confidence: 99%

4d Ultrafast Electron Diffraction, Crystallography, and Microscopy

Zewail

2006

Annu. Rev. Phys. Chem.

500

341

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■ Abstract In this review, we highlight the progress made in the development of 4D ultrafast electron diffraction (UED), crystallography (UEC), and microscopy (UEM) with a focus on concepts, methodologies, and prototypical applications. The joint atomic-scale resolutions in space and time, and sensitivity reached, make it possible to determine complex transient structures and assemblies in different phases. These applications include studies of isolated chemical reactions (molecular beams), interfaces, surfaces and nanocrystals, self-assembly, and 2D crystalline fatty-acid bilayers. In 4D UEM, we are now able, using timed, single-electron packets, to image nano-to-micro scale structures of materials and biological cells. Future applications of these methods are foreseen across areas of physics, chemistry, and biology.

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Section: Discussionmentioning

confidence: 99%

4d Ultrafast Electron Diffraction, Crystallography, and Microscopy

Zewail

2006

Annu. Rev. Phys. Chem.

500

341

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“…Subsequently, estimates of the number of particles needed for a reconstruction in the presence of noise have been proposed by taking into account the average SNR of the data (Glaeser, 1999;Rosenthal et al, 2003). Under the proposed theoretical formulation of Rosenthal and Henderson, we would expect to see a linear relationship in the plot of log (Nd) vs 1/d 2 , where N is the number of particles and d is the resolution.…”

Section: Relation Of Number Of Particles To Resolution In Single Partmentioning

confidence: 99%

Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-path Simulated Annealing optimization algorithm

Liu

Jiang

Jakana

et al. 2007

Journal of Structural Biology

112

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Accurately determining a cryoEM particle's alignment parameters is crucial to high resolution single particle 3-D reconstruction. We developed Multi-Path Simulated Annealing, a Monte Carlo type of optimization algorithm, for globally aligning the center and orientation of a particle simultaneously. A consistency criterion was developed to ensure the alignment parameters are correct and to remove some bad particles from a large pool of images of icosahedral particles. Without using any a priori model, this procedure is able to reconstruct a structure from a random initial model. Combining the procedure above with a new empirical double threshold particle selection method, we are able to pick tens of best quality particles to reconstruct a subnanometer resolution map from scratch. Using the best 62 particles of rice dwarf virus, the reconstruction reached 9.6Å resolution at which 4 helices of the P3A subunit of RDV are resolved. Furthermore, with the 284 best particles, the reconstruction is improved to 7.9Å resolution, and 21 of 22 helices and 6 of 7 beta sheets are resolved.

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“…X-ray diffraction, electron diffraction, and nuclear magnetic resonance (NMR) are well-established and powerful tools for the analysis of macromolecular structure with atomic precision, which with advances in technology, have continued to push the limits of the size and complexity of systems that can be structurally illuminated (Beauchamp and Isaacs, 1999;Chiu et al, 1999;Glaeser, 1999;Glusker, 1993;Henderson, 1995;Siegal et al, 1999;Stowell et al, 1998;Wuthrich, 1995). As one looks to the future, the needs for and impact of macromolecular structure analysis are expected to expand significantly in several areas, including: (1) increased throughput of structural analysis of gene products discovered by large scale genome sequencing (Kim, 1998); (2) routine characterization of large multimeric structures, such as protein assemblies and protein-nucleic acid complexes involved in signaling and regulation; and (3) understanding dynamic features of protein-protein and protein-nucleic acid assemblies.…”

Section: Introductionmentioning

confidence: 99%

Structural and functional imaging with carbon nanotube AFM probes

Hafner

Cheung

Woolley

et al. 2001

Progress in Biophysics and Molecular Biology

318

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Atomic force microscopy (AFM) has great potential as a tool for structural biology, a field in which there is increasing demand to characterize larger and more complex biomolecular systems. However, the poorly characterized silicon and silicon nitride probe tips currently employed in AFM limit its biological applications. Carbon nanotubes represent ideal AFM tip materials due to their small diameter, high aspect ratio, large Young's modulus, mechanical robustness, well-defined structure, and unique chemical properties. Nanotube probes were first fabricated by manual assembly, but more recent methods based on chemical vapor deposition provide higher resolution probes and are geared towards mass production, including recent developments that enable quantitative preparation of individual single-walled carbon nanotube tips [J. Phys. Chem. B 105 (2001) 743]. The high-resolution imaging capabilities of these nanotube AFM probes have been demonstrated on gold nanoparticles and well-characterized biomolecules such as IgG and GroES. Using the nanotube probes, new biological structures have been investigated in the areas of amyloid-beta protein aggregation and chromatin remodeling, and new biotechnologies have been developed such as AFM-based haplotyping. In addition to measuring topography, chemically functionalized AFM probes can measure the spatial arrangement of chemical functional groups in a sample. However, standard silicon and silicon nitride tips, once functionalized, do not yield sufficient resolution to allow combined structural and functional imaging of biomolecules. The unique end-group chemistry of carbon nanotubes, which can be arbitrarily modified by established chemical methods, has been exploited for chemical force microscopy, allowing single-molecule measurements with well-defined functionalized tips.

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Review: Electron Crystallography: Present Excitement, a Nod to the Past, Anticipating the Future

Cited by 139 publications

References 70 publications

4d Ultrafast Electron Diffraction, Crystallography, and Microscopy

4d Ultrafast Electron Diffraction, Crystallography, and Microscopy

Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-path Simulated Annealing optimization algorithm

Structural and functional imaging with carbon nanotube AFM probes

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