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X-RAY RUNS: Apply for Beamtime

2017  Nov 1 - Dec 21

2018  Feb 7 - Apr 3
2018  Proposal/BTR deadline: 12/1/17

2018  Apr 11 - Jun 4
2018  Proposal/BTR deadline: 2/1/18




WORKSHOP I: Structural Materials Opportunities for Combining Polycrystal Modeling and High Energy X-rays

Matt Miller, CHESS, Cornell University

High energy synchrotron x-rays can pass through bulk thicknesses of most engineering alloys - interrogating every crystal. Over the past decade, high speed area detectors and in-situ sample environments have enabled a new generation of synchrotron x-ray based alloy characterization experiments - probing the lattice orientations, lattice strains and topology for each crystal within a deforming polycrystal under a spectrum of processing and loading conditions. The current menu of techniques - including high energy x-ray diffraction (HEXD), diffuse scattering and computed tomography - have demonstrated the enormous potential of synchrotron x-rays for examining “real” engineering materials subjected to “real” engineering conditions. These measurements have created a significant opportunity and challenge for the materials modeling community. The physical relevance of the data and the huge volume of data being produced taxes the current generation of data reduction tools. Moreover, the “real time” aspect of the in situ experiments, make these data ideal for interfacing with a spectrum of structure-based micromechanical models. The speakers in this workshop will describe the details of interfacing finite element based polycrystal models with HEXD experiments with in situ loading. Topics include instantiation of virtual polycrystals and comparing experimental diffraction data with simulations. A range of engineering alloys: copper, titanium, stainless steel and aluminum will be described.

WORKSHOP II: Recent Applications in BioSAXS and New Developments in Combining SAXS and NMR Data

Alvin Acerbo, MacCHESS, Cornell University

Small Angle X-Ray Scattering (SAXS) is a method for investigating the structure and dynamics of biological macromolecules in solution at a low resolution. Whereas the applicability of traditional protein crystallography is limited to a subset of proteins, the versatility of bioSAXS makes it an attractive technique to study challenging macromolecular systems. The dramatic increase in popularity of bioSAXS has both been driven by and fueled the further development of instrumentation, data reconstruction algorithms and as well as the integration of data from bioSAXS and complementary techniques. Recent progress in these areas is paving the way for bioSAXS experiments on more challenging systems, such as multidomain proteins, protein complexes and polydisperse systems.

This year’s CHESS Users’ Meeting will feature a bioSAXS workshop focusing on recent applications of bioSAXS and new developments in combining data from bioSAXS and Nuclear Magnetic Resonance experiments. This workshop will begin with a brief overview of recent upgrades and capabilities of bioSAXS at MacCHESS, followed by talks from invited speakers.

immunoglobulin-like domain

NMR structure of an immunoglobulin-like domain along with a homology model of the neighboring immunoglobulin-like domain all within SAXS derived DAMMAVER and DAMFILT envelopes for the two domain constructs (image courtesy of C. Ptak, Oswald Group, Cornell).