Details

Autor(en) / Beteiligte

• MacDowell, Alastair A.
• Celestre, Rich 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, Tom
• Berger, James M.
• Agard, David A.
• Padmore, Howard A.

Titel

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

Ist Teil von

• Journal of synchrotron radiation, 2004-11, Vol.11 (6), p.447-455

Ort / Verlag

5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers

Erscheinungsjahr

2004

Link zum Volltext

Quelle

Wiley Online Library - AutoHoldings Journals

Beschreibungen/Notizen

• At the Advanced Light Source, three protein crystallography beamlines have been built that use as a source one of the three 6 T 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, owing 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.