Robert Glaeser

Modeling chemical bonding effects for protein electron crystallography: the transferable fragmental electrostatic potential (TFESP) method.

A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy.

Crystallization of membrane proteins from media composed of connected-bilayer gels.

Crystal structure of the bromide-bound D85S mutant of bacteriorhodopsin: principles of ion pumping.

Specificity of anion binding in the substrate pocket of bacteriorhodopsin.

Electron microscopy of biological macromolecules: bridging the gap between what physics allows and what we currently can get.

High-throughput film-densitometry: an efficient approach to generate large data sets.

Particle picking by segmentation: a comparative study with SPIDER-based manual particle picking.

The parallelization of SPIDER on distributed-memory computers using MPI.

Stroboscopic image capture: reducing the dose per frame by a factor of 30 does not prevent beam-induced specimen movement in paraffin.

SPARX, a new environment for Cryo-EM image processing.

Design of a microfabricated, two-electrode phase-contrast element suitable for electron microscopy.

Octomeric pyruvate-ferredoxin oxidoreductase from Desulfovibrio vulgaris.

Macromolecular structures without crystals.

Restoration of weak phase-contrast images recorded with a high degree of defocus: the "twin image" problem associated with CTF correction.

Retrospective: radiation damage and its associated "information limitations".

Retrospective on the early development of cryoelectron microscopy of macromolecules and a prospective on opportunities for the future.

Practical factors affecting the performance of a thin-film phase plate for transmission electron microscopy.

A method for the alignment of heterogeneous macromolecules from electron microscopy.

Experimental characterization and mitigation of specimen charging on thin films with one conducting layer.

Survey of large protein complexes in D. vulgaris reveals great structural diversity.

Precise beam-tilt alignment and collimation are required to minimize the phase error associated with coma in high-resolution cryo-EM.

The surface of evaporated carbon films is an insulating, high-bandgap material.

Reaching the information limit in cryo-EM of biological macromolecules: experimental aspects.

Design of a hybrid double-sideband/single-sideband (schlieren) objective aperture suitable for electron microscopy.

Human tripeptidyl peptidase II: a gentle giant.

Electron microscopy of biotinylated protein complexes bound to streptavidin monolayer crystals.

Electron microscopy of biological specimens in liquid water.

Deprotonation of D96 in bacteriorhodopsin opens the proton uptake pathway.

Ranking TEM cameras by their response to electron shot noise.

Minimizing electrostatic charging of an aperture used to produce in-focus phase contrast in the TEM.

Optimal and fast rotational alignment of volumes with missing data in Fourier space.

Replication and validation of cryo-EM structures.

Invited review article: Methods for imaging weak-phase objects in electron microscopy.

Generalization of the Matsumoto-Tonomura approximation for the phase shift within an open aperture.

Disulfide linkage and structure of highly stable yeast-derived virus-like particles of murine polyomavirus.

Automated particle correspondence and accurate tilt-axis detection in tilted-image pairs.

Factors that Influence the Formation and Stability of Thin, Cryo-EM Specimens.

How good can cryo-EM become?

Protein complexes in focus.

Long shelf-life streptavidin support-films suitable for electron microscopy of biological macromolecules.

Specimen Behavior in the Electron Beam.

Monolayer-crystal streptavidin support films provide an internal standard of cryo-EM image quality.

Multi-pass transmission electron microscopy.

Opinion: hazards faced by macromolecules when confined to thin aqueous films.

Estimating the effect of finite depth of field in single-particle cryo-EM.

How Cryo-EM Became so Hot.

PROTEINS, INTERFACES, AND CRYO-EM GRIDS.

How Good Can Single-Particle Cryo-EM Become? What Remains Before It Approaches Its Physical Limits?

Current outcomes when optimizing 'standard' sample preparation for single-particle cryo-EM.

Laser phase plate for transmission electron microscopy.

Microscale Fluid Behavior during Cryo-EM Sample Blotting.

Observation of the Relativistic Reversal of the Ponderomotive Potential.

Spectral DQE of the Volta phase plate.

Defocus-dependent Thon-ring fading.

Preparing Better Samples for Cryo-Electron Microscopy: Biochemical Challenges Do Not End with Isolation and Purification.

Minimizing Crinkling of Soft Specimens Using Holey Gold Films on Molybdenum Grids for Cryogenic Electron Microscopy.

High-power near-concentric Fabry-Perot cavity for phase contrast electron microscopy.

Simple assay for adsorption of proteins to the air-water interface.

Conquer by cryo-EM without physically dividing.

Perspective: Emerging strategies for determining atomic-resolution structures of macromolecular complexes within cells.

Perspective: Biochemical and Physical Constraints Associated With Preparing Thin Specimens for Single-Particle Cryo-EM.

Overcoming resolution loss due to thermal magnetic field fluctuations from phase plates in transmission electron microscopy.

Overcoming resolution loss due to thermal magnetic field fluctuations from phase plates in transmission electron microscopy.

Challenges in making ideal cryo-EM samples.

Overcoming Resolution Loss in Laser Phase Plate Cryo-Electron Microscopy.