Crystallization of the focal adhesion kinase targeting (FAT) domain in a primitive orthorhombic space group.
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.
Magis
Andrew T
AT
Department of Pathology, Immunology and Laboratory Medicine, University of Florida College of Medicine, 1600 SW Archer Road, Gainesville, FL 32610, USA.
Bailey
Kate M
KM
Kurenova
Elena V
EV
Hernández Prada
Jose A
JA
Cance
William G
WG
Ostrov
David A
DA
D000595:Amino Acid Sequence; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D051416:Focal Adhesion Protein-Tyrosine Kinases / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction
D051416:Focal Adhesion Protein-Tyrosine Kinases