Purification, crystallization and preliminary X-ray diffraction studies of Rab11 in complex with Rab11-FIP2

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Abstract

The small GTPase Rab11 regulates the recycling of endosomes back to the plasma membrane. In its active GTP-bound form, Rab11 binds a novel set of effectors termed the Rab11 family of interacting proteins (Rab11-FIPs) which contain a conserved C-terminal Rab-binding domain (RBD) of unknown structure. Here, a complex of Rab11 with the RBD of Rab11-FIP2 has been purified and crystallized in the trigonal space group P3121, with unit-cell parameters a = 64.99, b = 64.99, c = 112.59 Å. Static light-scattering analyses of the molecular weight of the complex in solution are consistent with two copies of Rab11 and two copies of Rab11-FIP2 in the complex. © 2006 International Union of Crystallography All rights reserved.

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Jagoe, W. N., Jackson, S. R., Lindsay, A. J., McCaffrey, M. W., & Khan, A. R. (2006). Purification, crystallization and preliminary X-ray diffraction studies of Rab11 in complex with Rab11-FIP2. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(7), 692–694. https://doi.org/10.1107/S1744309106023074

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