Microtubules (MT) are dynamic protein-based polymers with numerous applications in materials science including the active transport of nanomaterials and as templates for biomimetic materials synthesis. Some of these applications require that the dynamic nature of the MT be suppressed, and in this report we will discuss the preparation and stability of chemically crosslinked microtubules (CLMTs). MT reaction with gluteraldehyde results in the formation of protein dimers and higher molecular weight oligimers as observed by gel electrophoresis, confirming the formation of covalent inter-protein linkages. While extensive crosslinking was found to destabilize MTs and inactivate them with regards to kinesin binding, moderate amounts of crosslinking lead to CLMTs that had functional lifetimes of at least twice that of uncrosslinked MTs. Further studies demonstrated that CLMTs exhibited a wider thermal stability window and were far more resistant to metal-ion induced depolymerization than uncrosslinked MTs.