Mercury-induced crystallization and SAD phasing of the human Fe65-PTB1 domain
- Heidelberg University Biochemistry Center, INF328, D-69120 Heidelberg (Germany)
- 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, Vol. 64, Issue Pt 5; Other Information: PMCID: PMC2376396; PMID: 18453707; PUBLISHER-ID: en5289; OAI: oai:pubmedcentral.nih.gov:2376396; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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