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

Journal Article · Thu May 01 04:00:00 EDT 2008 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S174430910800835X· OSTI ID:22360561

Radzimanowski, Jens; Ravaud, Stéphanie ^[1]; Beyreuther, Konrad ^[2]; Sinning, Irmgard; Wild, Klemens ^[1]

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1. Heidelberg University Biochemistry Center, INF328, D-69120 Heidelberg (Germany)
2. Center for Molecular Biology, University Heidelberg, INF282, D-69120 Heidelberg (Germany)

Crystals of the phosphotyrosine-binding domain 1 (PTB1) of the neuronal adaptor protein Fe65 grown in the presence of a mercury derivative show a dramatic improvement in resolution, permitting SAD phasing. 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 P2{sub 1}2{sub 1}2{sub 1} diffracting to 2.2 Å resolution. SAD phases have been computed to the diffraction limit at the wavelength of maximum absorption (L{sub III} edge)

• OSTI ID: 22360561
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 5 Vol. 64; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
ABSORPTION
CRYSTALLIZATION
CRYSTALS
DIFFRACTION
DIFFUSION
MERCURY
PRECURSOR
PROTEINS
RESOLUTION
SPACE GROUPS
SYMMETRY
WAVELENGTHS