Crystallization of the focal adhesion kinase targeting (FAT) domain in a primitive orthorhombic space group.

ABSTRACT: X-ray diffraction data from the targeting (FAT) domain of focal adhesion kinase (FAK) were collected from a single crystal that diffracted to 1.99 A resolution and reduced to the primitive orthorhombic lattice. A single molecule was predicted to be present in the asymmetric unit based on the Matthews coefficient. The data were phased using molecular-replacement methods using an existing model of the FAK FAT domain. All structures of human focal adhesion kinase FAT domains solved to date have been solved in a C-centered orthorhombic space group.

SUBMITTER: Magis AT 

PROVIDER: S-EPMC2496861 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature