The Mu2e Crystal Calorimeter: An Overview

The Mu2e experiment at Fermilab will search for the standard model-forbidden, charged lepton flavour-violating conversion of a negative muon into an electron in the field of an aluminium nucleus. The distinctive signal signature is represented by a mono-energetic electron with an energy near the muon's rest mass. The experiment aims to improve the current single-event sensitivity by four orders of magnitude by means of a high-intensity pulsed muon beam and a high-precision tracking system. The electromagnetic calorimeter complements the tracker by providing high rejection power in muon to electron identification and a seed for track reconstruction while working in vacuum in presence of a 1 T axial magnetic field and in a harsh radiation environment. For 100 MeV electrons, the calorimeter should achieve: (a) a time resolution better than 0.5 ns, (b) an energy resolution <10%, and (c) a position resolution of 1 cm. The calorimeter design consists of two disks, each loaded with 674 undoped CsI crystals read out by two large-area arrays of UV-extended SiPMs and custom analogue and digital electronics. We describe here the status of construction for all calorimeter components and the performance measurements conducted on the large-sized prototype with electron beams and minimum ionizing particles at a cosmic ray test stand. A discussion of the calorimeter's engineering aspects and the on-going assembly is also reported

Mu2e Crystal Calorimeter Readout Electronics: Design and Characterisation

The Mu2e experiment at Fermi National Accelerator Laboratory will search for the charged-lepton flavour-violating neutrinoless conversion of negative muons into electrons in the Coulomb field of an Al nucleus. The conversion electron with a monoenergetic 104.967 MeV signature will be identified by a complementary measurement carried out by a high-resolution tracker and an electromagnetic calorimeter, improving by four orders of magnitude the current single-event sensitivity. The calorimeter—composed of 1348 pure CsI crystals arranged in two annular disks—has a high granularity, 10% energy resolution and 500 ps timing resolution for 100 MeV electrons. The readout, based on large-area UV-extended SiPMs, features a fully custom readout chain, from the analogue front-end electronics to the digitisation boards. The readout electronics design was validated for operation in vacuum and under magnetic fields. An extensive radiation hardness certification campaign certified the FEE design for doses up to 100 krad and 1012 n1MeVeq/cm2 and for single-event effects. A final vertical slice test on the final readout chain was carried out with cosmic rays on a large-scale calorimeter prototype

Structural Isosteres of Phosphate Groups in the Protein Data Bank

We developed a computational workflow to mine the Protein Data Bank for isosteric replacements that exist in different binding site environments but have not necessarily been identified and exploited in compound design. Taking phosphate groups as examples, the workflow was used to construct 157 data sets, each composed of a reference protein complexed with AMP, ADP, ATP, or pyrophosphate as well other ligands. Phosphate binding sites appear to have a high hydration content and large size, resulting in U-shaped bioactive conformations recurrently found across unrelated protein families. A total of 16 413 replacements were extracted, filtered for a significant structural overlap on phosphate groups, and sorted according to their SMILES codes. In addition to the classical isosteres of phosphate, such as carboxylate, sulfone, or sulfonamide, unexpected replacements that do not conserve charge or polarity, such as aryl, aliphatic, or positively charged groups, were found