The C-terminal domains of gammaS-crystallin pair about a distorted twofold axis

The 2-domain gammaS-crystallin, a highly conserved early evolutionaryoff-shoot of the gamma-crystallin family, is located in the water-richregion of eye lenses. The expressed C-terminal domain, gammaS-C, has beencrystallized and the 2.56 A X-ray structure determined. There are twodomains in the asymmetric unit which pair about a distorted twofold axis.One of the domains has an altered conformation in a highly conserved regionof the protein, the tyrosine corner. The distorted gammaS-C dimer ofdomains is compared with the highly symmetrical, equivalent recombinantdimer of C-terminal domains from gammaB- crystallin. Sequence changes closeto the interface, that distinguish gammaS from the other gamma-crystallins,are examined in order to evaluate their role in symmetrical domain pairing.     

Transformation calibration of a camera mounted on a robot

The paper describes the accurate calibration of the camera transformation for a vision system consisting of a camera mounted on a robot. The calibration includes an analysis of the linearity of the camera. A knowledge of the camera transformation allows the three-dimensional position of the object points to be determined using triangulation.     

Physical and functional interactions between the herpes simplex virus UL15 and UL28 DNA cleavage and packaging proteins

Herpes simplex virus (HSV) DNA is cleaved from concatemers and packaged into capsids in infected cell nuclei. This process requires seven viral proteins, including UL15 and UL28. UL15 expressed alone displays a nuclear localization, while UL28 remains cytoplasmic. Coexpression with UL15 enables UL28 to enter nuclei, suggesting an interaction between the two proteins. Additionally, UL28 copurified with UL15 from HSV-infected cells after ion-exchange and DNA affinity chromatography, and the complex sedimented as a 1:1 heterodimer upon sucrose gradient centrifugation. These findings are evidence of a physical interaction of UL15 and UL28 and a functional role for UL15 in directing UL28 to the nucleus.