Crystal Structure of the KIF5C Motor Domain Without Any Nucleotide

X-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding

MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNG
TIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDK
NRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVS
KTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMF
GQRAKTIKNTVSVNHHHHHHH

Ammonium sulfate, Sodium citrate, Glycerol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES: REFINED INDIVIDUALLY

kinesin, motor domain, nucleotide-free, motor protein, ATPase, nucleotide binding, microtubule, transport protein

MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNG
TIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDK
NRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVS
KTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMF
GQRAKTIKNTVSVN