Microtubules are non-covalent polymers formed from heterodimers of α- and β- tubulin molecules. These polymers play a significant role in cell function, such as the formation of the mitotic spindle for chromosome segregation, the formation of flagella and cilia to allow movement and are one of the main components of the cell cytoskeleton, which gives cells their shape and allow intracellular transport of organelles. Numerous disease-associated point mutations have been found present on different tubulin genes causing a spectrum of neurodevelopmental disorder diseases, such as lissencephaly (smooth brain), polymicrogyria, and cortical malformations, collectively known as tubulinopathies (Cushion et al., 2023). Due to the difficulty of generating pure recombinant mutant tubulins, a knowledge gap still exists in the acting mechanism of these disease-causing mutations. In this research, we will purify and characterise two disease-related mutations, L286F on α-tubulin, related to lissencephaly (smooth brain) and D417H mutation on β-tubulin, causing ocular motility disorder CFEOM3, using MEC-12 and MEC-7 tubulins found in mechanosensory neurons of C. elegans. We successfully generated recombinant MEC-12L286F and MEC-7D417H using the insect cell-based protein expression system. The next step is to purify the mutant tubulins, which willallow in vitro assays to study the microtubule dynamics and the interactions with microtubule-associated proteins and motors, leading to possible future in vivo studies.