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Title
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Mercury-induced crystallization and SAD phasing of the human Fe65-PTB1 domain.
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Authors
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J.Radzimanowski,
S.Ravaud,
K.Beyreuther,
I.Sinning,
K.Wild.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008,
64,
382-385.
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PubMed id
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Abstract
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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 A 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
P2(1)2(1)2(1) diffracting to 2.2 A resolution. SAD phases have been computed to
the diffraction limit at the wavelength of maximum absorption (L(III) edge).
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