EC Number |
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5.6.1.1 | crystals of spastin are grown using the vapor diffusion method at 20°C |
5.6.1.1 | hanging drop method, the N-terminal residues (about 10000 Da) are clipped off during time of crystal formation (5-7 days) |
5.6.1.1 | hanging-drop method at 20°C, crystal structure of KATNAL1 AAA ATPase in the nucleotide-free state reveals a monomer |
5.6.1.1 | hanging-drop method at 20°C, crystal structure of MEI-1 AAA ATPase in the ADP-bound state reveals a pseudo-hexameric left-handed spiral assembly |
5.6.1.1 | high-resolution structure of the heterodimeric complex of p60-microtubule interacting and trafficking domain and the p80 C-terminal domain is determined by X-ray crystallography |
5.6.1.1 | secondary structure analyzed by circular dichroism (CD) spectrum. SPAS-1 retains a high degree of alpha-helical structure |
5.6.1.1 | the structure of kp60-NTD reveals a striking similarity to those of the microtubule interacting and trafficking domains (MIT). The arragnement of helices 2 and 3 is well conserved between kp60-NTD and the MIT domain from Vps4, a homologous protein that promotes disassembly of the endosomal sorting complexes required for transport III membrane skeleton complex. The positively charged surface formed by helices 2 and 3 binds tubulin |
5.6.1.1 | the X-ray structure of the nucleotide-free, monomeric AAA domain of Drosophila melanogaster spastin, residues 464-758, is solved at a resolution of 2.7 A |