Results from the Antarctic Muon and Neutrino Detector Array (AMANDA)

We show new results from both the older and newer incarnations of AMANDA (AMANDA-B10 and AMANDA-II, respectively). These results demonstrate that AMANDA is a functioning, multipurpose detector with significant physics and astrophysics reach. They include a new higher-statistics measurement of the atmospheric muon neutrino flux and preliminary results from searches for a variety of sources of ultrahigh energy neutrinos: generic point sources, gamma-ray bursters and diffuse sources producing muons in the detector, and diffuse sources producing electromagnetic or hadronic showers in or near the detector.Comment: Invited talk at the XXth International Conference on Neutrino Physics and Astrophysics (Neutrino 2002), Munich, Germany, May 25-30, 200

Electron density for NAG bound to lysozyme and for ASN bound to thermolysin.

<p>Panel A: N-acetyl glucosamine is shown bound to lysozyme (difference omit map is contoured at 3.0 σ). The lysozyme data comes from a 310 µm crystal that was soaked for 750 seconds, with a refined occupancy of 74% and occupancy calculated using Eq. 1 of 68%. Panel B: Asparagine is shown bound to thermolysin (difference omit map is countered at 3.0 σ). The thermolysin data comes from a 220 µm crystal that was soaked for 601 seconds, with a refined occupancy of 99% and occupancy calculated using Eq. 1 of 84%.</p

Crystallization conditions.

<p>Crystallization conditions.</p

Refined occupancies (y axes, %) as a function of soak time (x axes, seconds).

<p>Two dimensional slices are shown for the three dimensional relationship between crystal size, ligand soak time, and occupancy (O_calc and O_refine). In each panel, the crystal size variable is excluded by grouping crystals of similar sizes. Lysozyme + NAG crystals are grouped by size (0–60 µm in box <b>A</b>, 60–120 µm in box <b>B</b>, 120–180 µm in box <b>C</b>, 180–240 µm in box <b>D</b>, 240–360 µm in box <b>E</b>, 360–480 µm in box <b>F</b>). Thermolysin + asparagine crystals are grouped into two sizes (0–150 µm in box <b>α</b>, and 150–300 µm in box <b>β</b>). Each data point represents the observed soak time and occupancy of one crystal + ligand. The average size for crystals in each range is indicated. The average number of calculated structure factors that were added into the data () is also shown (larger crystals had more overloads and consequently more added reflections). Inspection of the relationship between soak time and refined occupancy revealed a linear relationship between crystal length and the time needed to reach 50% maximum occupancy (t_1/2), so that t_1/2 = Lτ, where L is the crystal length and τ is a fixed constant. Best fits for lysozyme (R² = 78%) and thermolysin (R² = 88%) were calculated using least squares applied to Eq. 1. In each panel, a solid line shows Eq. 1 with the average size of crystals in that panel assigned to L (fitting parameters taken from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0101036#pone-0101036-t002" target="_blank">Table 2</a>). Note that the data in each panel come from crystals with similar but not identical sizes. Consequently, the data fit Eq. 1 much better than these graphs suggest. The average residual between calculated occupancies from Eq. 1 and refined occupancies from the X-ray diffraction data was 9.76% for lysozyme + NAG and 6.51% for thermolysin + ASN.</p