Measurement of the ATLAS solenoid magnetic field

ATLAS is a general purpose detector designed to explore a wide range of physics at the Large Hadron Collider. At the centre of ATLAS is a tracking detector in a 2 T solenoidal magnetic field. This paper describes the machine built to map the field, the data analysis methods, the final results, and their estimated uncertainties. The remotely controlled mapping machine used pneumatic motors with feedback from optical encoders to scan an array of Hall probes over the field volume and log data at more than 20 000 points in a few hours. The data were analysed, making full use of the physical constraints on the field and of our knowledge of the solenoid coil geometry. After a series of small corrections derived from the data itself, the resulting maps were fitted with a function obeying Maxwell's equations. The fit residuals had an r.m.s. less than 0.5 mT and the systematic error on the measurement of track sagitta due to the field uncertainty was estimated to be in the range 0.02 % to 0.12 % depending on the track rapidity

Measurement of the solenoid magnetic field

We describe the machine used to map the solenoid field and the data sets that were collected. The bulk of the note describes the analysis of this data. A series of small corrections are made; some taken from surveys and some derived from the data itself. Two fitting methods are defined and applied to all data sets. The final result is that the field map at normal operating current can be fitted to a function that obeys Maxwell with an r.m.s. residual of less than 5 Gauss. Systematic errors on the measurement of track sagitta due to the field uncertainty are estimated to be in the range 2.3E-4 to 12E-4, depending on the track rapidity. Finally, the representation of the map in Athena is briefly described

EGFR oligomerization organizes kinase-active dimers into competent signalling platforms

Epidermal growth factor receptor (EGFR) signalling is activated by ligand-induced receptor dimerization. Notably, ligand binding also induces EGFR oligomerization, but the structures and functions of the oligomers are poorly understood. Here, we use fluorophore localization imaging with photobleaching to probe the structure of EGFR oligomers. We find that at physiological epidermal growth factor (EGF) concentrations, EGFR assembles into oligomers, as indicated by pairwise distances of receptor-bound fluorophore-conjugated EGF ligands. The pairwise ligand distances correspond well with the predictions of our structural model of the oligomers constructed from molecular dynamics simulations. The model suggests that oligomerization is mediated extracellularly by unoccupied ligand-binding sites and that oligomerization organizes kinase-active dimers in ways optimal for auto-phosphorylation in trans between neighbouring dimers. We argue that ligand-induced oligomerization is essential to the regulation of EGFR signalling