Kazuya Hasegawa
Protein Crystal Analysis Division, SPring-8/JASRI
E-mail: kazuya@spring8.or.jp
Abstract
In this presentation, I would like to talk about brief introduction of MX beamlines at SPring-8 as well as the recent activity of SPring-8 BL41XU. BL41XU started operation in 1997 just after official user operation of SPring-8. Since then the targets for structural study have become more challenging. In order to cope with such targets, we replaced the focusing optics and installed a new diffractometer during 2013 and 2014. The new optics adopt two-step focusing which provide beam size of 5×4 – 45×22 µm2 and photon flux of 2.3 × 1012 – 1.1×1013 (photons/s@12.4keV) in usual operation. The PILATUS3 6M facilitates rapid data collections in combination with the high flux beam. This upgrade led to the successful structure determination of difficult targets such as Cas9, GPCRs etc. In order to further increase the productivity, the sample changer was upgraded in this year; the time for sample exchange can be reduced to 13 s. Moreover, an automated data collection system ZOO, developed at micro-focus beamline BL32XU (Hirata, Yamashita in preparation), has been installed and will be available for users from this autumn. One unique feature of BL41XU is it allows for using high-energy X-ray, 20 to 35 keV; it is suitable for ultra-high resolution data collections (Hirano et al., 2016) and use of anomalous nuclei that has absorption edges in this range. The upgrade of diffractometer for the high-energy mode is ongoing. Finally, I would like to talk about unique result obtained at BL41XU: Visualizing the entire first layer of phospholipids surrounding transmembrane helices of Ca2+- ATPase by X-ray solvent contrast modulation (Norimatsu et al., 2017).
Hirano, Y., Takeda, K. & Miki, K. (2016). Nature. 534, 281–284.
Norimatsu, Y., Hasegawa, K., Shimizu, N. & Toyoshima, C. (2017). Nature. 545, 193–198.
