Mobile learning : structures, agency, practices

The main physics program of the International Linear Collider requires a measurement of the beam energy with a relative precision of the order 10(-4) or better. A magnetic spectrometer using high resolution beam position monitors (BPMs) has been proposed to achieve this goal. A prototype spectrometer chicane employing four dipole magnets is currently under development at the End Station A in SLAC, intending to demonstrate the required resolution and stability of this method and investigate possible systematic effects and operational issues. This contribution reports on the successful commissioning of the beam position monitor system and the resolution and stability achieved. Also, the initial results from a run with a full spectrometer chicane are presented

Results from a prototype chicane-based energy spectrometer for a Linear Collider

The International Linear Collider (ILC) and other proposed high energy e(+) e(-) machines aim to measure with unprecedented precision Standard Model quantities and new, not yet discovered phenomena. One of the main requirements for achieving this goal is a measurement of the incident beam energy with an uncertainty close to 10(-4). This article presents the analysis of data from a prototype energy spectrometer commissioned in 2006-2007 in SLAC's End Station A beamline. The prototype was a 4-magnet chicane equipped with beam position monitors measuring small changes of the beam orbit through the chicane at different beam energies. A single bunch energy resolution close to 5 . 10(-4) was measured, which is satisfactory for most scenarios. We also report on the operational experience with the chicane-based spectrometer and suggest ways of improving its performance

Results from a Prototype Chicane-Based Energy Spectrometer for a Linear Collider

The International Linear Collider and other proposed high energy e+ e- machines aim to measure with unprecedented precision Standard Model quantities and new, not yet discovered phenomena. One of the main requirements for achieving this goal is a measurement of the incident beam energy with an uncertainty close to 1e-4. This article presents the analysis of data from a prototype energy spectrometer commissioned in 2006--2007 in SLAC's End Station A beamline. The prototype was a 4-magnet chicane equipped with beam position monitors measuring small changes of the beam orbit through the chicane at different beam energies. A single bunch energy resolution close to 5e-4 was measured, which is satisfactory for most scenarios. We also report on the operational experience with the chicane-based spectrometer and suggest ways of improving its performance.Comment: To be submitted to Journal of Instrumentatio

Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase.

Propionyl-coenzyme A carboxylase (PCC), a mitochondrial biotin-dependent enzyme, is essential for the catabolism of the amino acids Thr, Val, Ile and Met, cholesterol and fatty acids with an odd number of carbon atoms. Deficiencies in PCC activity in humans are linked to the disease propionic acidaemia, an autosomal recessive disorder that can be fatal in infants. The holoenzyme of PCC is an alpha(6)beta(6) dodecamer, with a molecular mass of 750 kDa. The alpha-subunit contains the biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) domains, whereas the beta-subunit supplies the carboxyltransferase (CT) activity. Here we report the crystal structure at 3.2-A resolution of a bacterial PCC alpha(6)beta(6) holoenzyme as well as cryo-electron microscopy (cryo-EM) reconstruction at 15-A resolution demonstrating a similar structure for human PCC. The structure defines the overall architecture of PCC and reveals unexpectedly that the alpha-subunits are arranged as monomers in the holoenzyme, decorating a central beta(6) hexamer. A hitherto unrecognized domain in the alpha-subunit, formed by residues between the BC and BCCP domains, is crucial for interactions with the beta-subunit. We have named it the BT domain. The structure reveals for the first time the relative positions of the BC and CT active sites in the holoenzyme. They are separated by approximately 55 A, indicating that the entire BCCP domain must translocate during catalysis. The BCCP domain is located in the active site of the beta-subunit in the current structure, providing insight for its involvement in the CT reaction. The structural information establishes a molecular basis for understanding the large collection of disease-causing mutations in PCC and is relevant for the holoenzymes of other biotin-dependent carboxylases, including 3-methylcrotonyl-CoA carboxylase (MCC) and eukaryotic acetyl-CoA carboxylase (ACC)