Suite of three protein crystallography beamlines with single superconducting bend magnet as the source
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Suite of three protein crystallography beamlines with single superconducting bend magnet as the source

  • Author(s): MacDowell, Alastair A.
  • Celestre, Richard S.
  • Howells, Malcolm
  • McKinney, Wayne
  • Krupnick, James
  • Cambie, Daniella
  • Domning, Edward E
  • Duarte, Robert M.
  • Kelez, Nicholas
  • Plate, David W.
  • Cork, Carl W.
  • Earnest, Thomas N.
  • Dickert, Jeffery
  • Meigs, George
  • Ralston, Corie
  • Holton, James M.
  • Alber, Thomas
  • Berger, James M.
  • Agard, David A.
  • Padmore, Howard A.
  • et al.
Abstract

At the Advanced Light Source (ALS), three protein crystallography (PX) beamlines have been built that use as a source one of the three 6 Tesla single pole superconducting bending magnets (superbends) that were recently installed in the ring. The use of such single pole superconducting bend magnets enables the development of a hard x-ray program on a relatively low energy 1.9 GeV ring without taking up insertion device straight sections. The source is of relatively low power, but due to the small electron beam emittance, it has high brightness. X-ray optics are required to preserve the brightness and to match the illumination requirements for protein crystallography. This was achieved by means of a collimating premirror bent to a plane parabola, a double crystal monochromator followed by a toroidal mirror that focuses in the horizontal direction with a 2:1 demagnification. This optical arrangement partially balances aberrations from the collimating and toroidal mirrors such that a tight focused spot size is achieved. The optical properties of the beamline are an excellent match to those required by the small protein crystals that are typically measured. The design and performance of these new beamlines are described.

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