A TOG:  -tubulin Complex Structure Reveals Conformation-Based Mechanisms for a Microtubule Polymerase

Design, Overexpression, and Purification of Polymerization-Blocked Yeast αβ-Tubulin Mutants

(2011) Vinu Johnson et al.   BIOCHEMISTRY

XMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region

(2011) P. O. Widlund et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

XMAP215 Is a Processive Microtubule Polymerase

(2008) Gary J. Brouhard et al.   CELL

Mal3, the Schizosaccharomyces pombe homolog of EB1, changes the microtubule lattice

(2008) Amédée des Georges et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The lattice as allosteric effector: Structural studies of   - and  -tubulin clarify the role of GTP in microtubule assembly

(2008) L. M. Rice et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA