Crystallization and phasing of focal adhesion protein 52 from Gallus gallus

Authors: Törő, Imre; Nikki, Marko; Glumoff, Tuomo; Lehto, Veli-Pekka; Djinović Carugo, Kristina

Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 539-541(3)

Publisher: Blackwell Publishing

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Abstract:

Focal adhesion protein 52 (FAP52) is a multidomain adaptor protein of 448 amino acids characterized as an abundant component of focal adhesions. FAP52 binds to filamin via its N-terminal α-helical domain, suggesting a role in linking focal adhesions to the actin-based cytoskeleton. The recombinant protein was crystallized using the hanging-drop vapour-diffusion method, which yielded two crystal forms. Native data were collected from both crystal forms to 2.8 and 2.1 Å resolution, respectively. For one of the crystal forms, initial MAD phasing was successfully performed using two data sets from xenon-derivatized crystals. The derivative data sets were collected using softer X-rays of 1.5 and 1.9 Å wavelength. Preliminary structural analysis reveals the presence of a dimer in the asymmetric unit.

Document Type: Research article

DOI: 10.1107/S090744490302907X

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