Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 5 (May 2008)

crystallization communications

Acta Cryst. (2008). F64, 382-385 [ doi:10.1107/S174430910800835X ]

Mercury-induced crystallization and SAD phasing of the human Fe65-PTB1 domain

J. Radzimanowski, S. Ravaud, K. Beyreuther, I. Sinning and K. Wild

Abstract: Fe65 is a three-domain neuronal adaptor protein involved in brain development and amyloid precursor protein (APP) signalling. The phosphotyrosine-binding domain 1 (PTB1) of human Fe65 has been cloned, overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method. Native crystals belong to the space group R3 and diffract to 2.6 Å resolution. This crystal form suffered from high thermal B factors and pseudo-symmetry, resulting in a bisection of the c axis. Co-crystallization with a mercury compound under similar conditions induced an orthorhombic crystal form in the space group P2₁2₁2₁ diffracting to 2.2 Å resolution. SAD phases have been computed to the diffraction limit at the wavelength of maximum absorption (L_III edge).

Keywords: Alzheimer's disease; amyloid precursor protein; Fe65; phosphotyrosine-binding domain.