MS02-P05 Present status of SPring-8 macromolecular crystallography beamlines Hideo Okumura (Protein Crystal Analysis Division, Japan Synchrotron Radiation Research Institute (JASRI), Sayo, Hyogo, Japan) Kazuya Hasegawa (Protein Crystal Analysis Division, Japan Synchrotron Radiation Research Institute (JASRI), Sayo, Hyogo, Japan) Seiki Baba (Protein Crystal Analysis Division, Japan Synchrotron Radiation Research Institute (JASRI), Sayo, Hyogo, Japan) Nobuhiro Mizuno (Protein Crystal Analysis Division, Japan Synchrotron Radiation Research Institute (JASRI), Sayo, Hyogo, Japan) Hironori Murakami (Protein Crystal Analysis Division, Japan Synchrotron Radiation Research Institute (JASRI), Sayo, Hyogo, Japan) Takashi Kumasaka (Protein Crystal Analysis Division, Japan Synchrotron Radiation Research Institute (JASRI), Sayo, Hyogo, Japan) Kunio Hirata (Advanced Photon Technology Division, RIKEN SPring-8 Center, Sayo, Hyogo, Japan) Go Ueno (Advanced Photon Technology Division, RIKEN SPring-8 Center, Sayo, Hyogo, Japan) Masaki Yamamoto (Advanced Photon Technology Division, RIKEN SPring-8 Center, Sayo, Hyogo, Japan)email: okumurah@spring8.or.jpAt SPring-8, JASRI and RIKEN are collaboratively developing five beamlines dedicated to macromolecular crystallography. Each beamline shares to serve broad requests from beamline users and liaises to develop new applications for enhancing each characteristic property.
Undulator beamlines, BL41XU [1] and BL32XU [2], focus on cutting edge analyses exploiting high flux microbeam produced by high-magnification focusing optics. In BL41XU, the two step focusing achieved beam size of 2 μm × 2 μm - 35 μm (H) × 50 μm (V). The wide range of beam size allows both micro-crystallography and high-resolution data collection that makes efficient use of crystal diffraction volume. In addition to high-resolution analysis, ultra-high resolution (~0.4 Å) data could be collected by using higher energy X-rays in energy range of 20 keV to 35 keV focused by using compound refractive lenses. Meanwhile, BL32XU can provide the fine beam with typical horizontal size of 1 μm. This micro-beam is very suited to data collection from small crystals, especially membrane protein crystals grown in LCP that are important targets on the beamline. For such micro-crystals, we developed an automated data collection system, ZOO. It is performed in advance of multi-crystal data collection for microcrystals; the crystal alignment tool, SHIKA, provides 2D spot population map of raster scan, and KUMA program is a tool suggesting data collection strategy with mitigating radiation damage.
On the other hand, the bending magnet beamlines BL26B1/B2 and BL38B1 are focused for automation and routine data collection exploiting stable and easily tunable beam. The humidifiers have been installed for the HAG (Humid Air and Glue-coating) mounting method [3], which involves a combination of controlled humid air and water-soluble polymer glue for crystal coating. By this technique, most protein crystals can be kept at room temperature and are able to be cryo-cooled under optimized humidity. In Situ X-ray diffraction instruments using crystallization plate have also been developing. This system consists of plate goniometer, robot arm for plate mounting and plate hotel.
 
References:

[1] Hasegawa, K. et al. (2013). J. Synchrotron Rad. 20, 910-913.

[2] Hirata, H. et al. (2013). J. Phys.: Conf. Ser. 425, 1-4.

[3] Baba, S. et al. (2013). Acta Cryst. D69, 1839-1849.
Keywords: synchrotron x-ray crystallgoraphy, macromolecular crystallography