Crystallization of the Focal Adhesion Kinase Targeting (FAT) Domain in a Primitive Orthorhombic Space Group

Journal Article · Tue Jan 01 00:00:00 EST 2008 · Acta Crystallographica Section F: Structural Biology and Crystallization Communications

DOI:https://doi.org/10.1107/S1744309108011421· OSTI ID:960088

Magis, A; Bailey, K; Kurenova, E; Hernandez Prada, J; Cance, W; Ostrov, D

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 Angstroms 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.

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 960088
• Report Number(s): BNL-83074-2009-JA; TRN: US201016%%1232
• Journal Information: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 64
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
ADHESION
CRYSTALLIZATION
FATS
MONOCRYSTALS
ORTHORHOMBIC LATTICES
PHOSPHOTRANSFERASES
RESOLUTION
SPACE GROUPS
X-RAY DIFFRACTION
national synchrotron light source