Miroslava Schaffer

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We present a fully automated method for three-dimensional (3D) elemental analysis demonstrated using a ceramic sample of chemistry (Ca)MgTiO(x). The specimen is serially sectioned by a focused ion beam (FIB) microscope, and energy-dispersive X-ray spectrometry (EDXS) is used for elemental analysis of each cross-section created. A 3D elemental model is(More)
We acquired molecular-resolution structures of the Golgi within its native cellular environment. Vitreous Chlamydomonas cells were thinned by cryo-focused ion beam milling and then visualized by cryo-electron tomography. These tomograms revealed structures within the Golgi cisternae that have not been seen before. Narrow trans-Golgi lumina were spanned by(More)
The molecular organization of eukaryotic nuclear volumes remains largely unexplored. Here we combined recent developments in cryo-electron tomography (cryo-ET) to produce three-dimensional snapshots of the HeLa cell nuclear periphery. Subtomogram averaging and classification of ribosomes revealed the native structure and organization of the cytoplasmic(More)
Chloroplast function is orchestrated by the organelle's intricate architecture. By combining cryo-focused ion beam milling of vitreous Chlamydomonas cells with cryo-electron tomography, we acquired three-dimensional structures of the chloroplast in its native state within the cell. Chloroplast envelope inner membrane invaginations were frequently found in(More)
Cryo-electron tomography (CET) is ideally suited for bridging the resolution gap between molecular and cellular structural studies. However, CET is limited to a sample thickness under 500nm, which is thinner than most cells. Here, we review a method for preparing cells for CET using focused-ion-beam milling, a technique commonly used in materials science.(More)
Correlative microscopy allows imaging of the same feature over multiple length scales, combining light microscopy with high resolution information provided by electron microscopy. We demonstrate two procedures for coordinate transformation based correlative microscopy of vitrified biological samples applicable to different imaging modes. The first procedure(More)
Imaging of fully hydrated, vitrified biological samples by electron tomography yields structural information about cellular protein complexes in situ. Here we present a computational procedure that removes artifacts of three-dimensional reconstruction caused by contamination present in samples during imaging by electron microscopy. Applying the procedure to(More)
While FIB sample preparation for transmission electron microscopy is a well established technique, few examples exist of samples of sufficient quality for atomic resolution imaging by aberration corrected (scanning) transmission electron microscopy (STEM). In this work we demonstrate the successful preparation of such samples from five different materials(More)
This work presents results from high-resolution scanning transmission electron microscopy and electron energy-loss spectroscopy on twin boundaries (TBs) and nontwin grain boundaries (GBs) in Cu(In,Ga)Se(2) thin films. It is shown that the atomic reconstruction is different for different symmetries of the grain boundaries. We are able to confirm the model(More)
While cryo-electron tomography (cryo-ET) can reveal biological structures in their native state within the cellular environment, it requires the production of high-quality frozen-hydrated sections that are thinner than 300nm. Sample requirements are even more stringent for the visualization of membrane-bound protein complexes within dense cellular regions.(More)