The mechano-enzyme dynamin-related protein 1 plays an important role in 
mitochondrial fission and is implicated in cell physiology. Dysregulation of 
Drp1 is associated with abnormal mitochondrial dynamics and neuronal damage. 
Drp1 shares structural and functional similarities with dynamin 1 with respect 
to domain organization, ability to self-assemble into spiral-like oligomers and 
GTP-cycle-dependent membrane scission. Structural studies of human dynamin-1 
have greatly improved the understanding of this prototypical member of the 
dynamin superfamily. However, high-resolution structural information for 
full-length human Drp1 covering the GTPase domain, the middle domain and the 
GTPase effector domain (GED) is still lacking. In order to obtain mechanistic 
insights into the catalytic activity, a nucleotide-free GTPase-GED fusion 
protein of human Drp1 was expressed, purified and crystallized. Initial X-ray 
diffraction experiments yielded data to 2.67 Å resolution. The hexagonal-shaped 
crystals belonged to space group P2(1)2(1)2, with unit-cell parameters a = 
53.59, b = 151.65, c = 43.53 Å, one molecule per asymmetric unit and a solvent 
content of 42%. Expression of selenomethionine-labelled protein is currently in 
progress. Here, the expression, purification, crystallization and X-ray 
diffraction analysis of the Drp1 GTPase-GED fusion protein are presented, which 
form a basis for more detailed structural and biophysical analysis.