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

Authors
  • Radzimanowski, Jens
  • Ravaud, Stéphanie
  • Beyreuther, Konrad
  • Sinning, Irmgard
  • Wild, Klemens
Type
Published Article
Journal
Acta Crystallographica Section F Structural Biology and Crystallization Communications
Publisher
International Union of Crystallography
Publication Date
May 01, 2008
Volume
64
Issue
Pt 5
Pages
382–385
Identifiers
DOI: 10.1107/S174430910800835X
PMID: 18453707
Source
Medline
License
Unknown

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 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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