A Major Conformational Change in p97 AAA ATPase upon ATP Binding.

Leginon: An Utomated System for Acquisition of Images from Vitreous Ice Specimens.

The Way Things Move: Looking Under the Hood of Molecular Motor Proteins.

A structural change in the kinesin motor protein that drives motility.

Myosin VI is an actin-based motor that moves backwards.

Structure and function of a membrane-bound murine MHC class I molecule.

Situs: A package for docking crystal structures into low-resolution maps from Electron Microscopy.

The motor protein myosin-I produces its working stroke in two steps.

Motor protein decoration of microtubules grown in high salt conditions reveals the presence of mixed lattices.

Characterization of two related drosophila gamma-tubulin complexes that differ in their ability to nucleate microtubules.

High-resolution model of the microtubule.

Self-organizing neural networks bridge the biomolecular resolution gap.

Lipid nanotubes as substrates for helical crystallization of macromolecules.

Three-dimensional structure of Acanthamoeba castellanii myosin-IB (MIB) determined by cryoelectron microscopy of decorated actin filaments.

Kinetic characterization of brush border myosin-I ATPase.

Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis.

Programs for visualization in three-dimensional microscopy.

Fine tuning a molecular motor: the location of alternative domains in the Drosophila myosin head.

A model for the microtubule-Ncd motor protein complex obtained by cryo-electron microscopy and image analysis.

Conformational changes due to calcium-induced calmodulin dissociation in brush border myosin I-decorated F-actin revealed by cryoelectron microscopy and image analysis.

Three different approaches for calculating the three-dimensional structure of microtubules decorated with kinesin motor domains.

Three-dimensional structure of Brush Border Myosin-I at approximately 20 A resolution by electron microscopy and image analysis.

Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry.

Two-dimensional crystallization of brush border myosin I.

Polarity of 2-D and 3-D maps of tubulin sheets and motor-decorated sheets.

Three-dimensional structure of ncd-decorated microtubules obtained by a back-projection method.

Protein-protein interactions in the rigor actomyosin complex.

Helical processing using PHOELIX.

A 32 degree tail swing in brush border myosin I on ADP release.

A 35-A movement of smooth muscle myosin on ADP release.

Toward understanding the structure and interactions of microtubules and motor proteins.

Three-dimensional structure of a tubulin-motor-protein complex.

PHOELIX: a package for semi-automated helical reconstruction.

Tubulin GTP hydrolysis influences the structure, mechanical properties, and kinesin-driven transport of microtubules.

Self-assembling organic nanotubes based on a cyclic peptide architecture.

Structure of the actin-myosin complex and its implications for muscle contraction.

Kinesin follows the microtubule's protofilament axis.

A comparison of the atomic model of F-actin with cryo-electron micrographs of actin and decorated actin.

Architecture and design of the nuclear pore complex.

Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study.

Cryo-electron microscopy of S1-decorated actin filaments.

Molecular structure of F-actin and location of surface binding sites.