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Harima Chemicals Group Inc spring-8 bl44xu beamline
Spring 8 Bl44xu Beamline, supplied by Harima Chemicals Group Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/spring-8/beamline+bl44xu/pmc12081879-277-22-25
Average 90 stars, based on 1 article reviews
spring-8 bl44xu beamline - by Bioz Stars, 2026-10
90/100 stars

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Article Title: Accelerator-based X-ray sources: synchrotron radiation, X-ray free electron lasers and beyond.
Article Snippet: The evolution of synchrotron radiation (SR) sources and related sciences is discussed to explain the ‘generation’ of the SR sources.. Most of the contemporary SR sources belong to the third generation, where the storage rings are optimized for the use of undulator radiation.. The undulator development allowed to reduction of the electron energy of the storage ring necessary for delivering 10 keV X-rays from the initial 6–8 GeV to the current 3 Gev.

Article Title: Investigating the Effect of Substituting a Single Cysteine Residue on the Thermal Stability of an Engineered Sweet Protein, Single-Chain Monellin
Article Snippet: X-ray diffraction data were collected at the SPring-8 (Harima, Japan) beamline of BL41XU at a wavelength of 1.0000 Å using an EIGER X 16 M (DECTRIS) detector using the ZOO automatic data collection system [ ].

Article Title: ATP-dependent polymerization dynamics of bacterial actin proteins involved in Spiroplasma swimming
Article Snippet: X-ray diffraction data were measured at 100 K at synchrotron beamlines BL41XU and BL45XU at SPring-8 (Harima, Japan) with the approval of the Japan Synchrotron Radiation Research Institute (JASRI) (proposal nos.

Article Title: Distance Distribution between Two Iodine Atoms Derived from Small-Angle X-ray Scattering Interferometry for Analyzing a Conformational Ensemble of Heavy Atom-Labeled Small Molecules.
Article Snippet: To obtain unbiased information on the dynamic conformational ensemble of a molecule in solution, one promising approach is small-angle X-ray scattering (SAXS).. Conventionally, SAXS data are converted to a pair distribution function, which describes the distance distribution between all pairs of atoms within a molecule.. If two strong X-ray scatterers are introduced and the background contributions from the other atoms are suppressed, then the distance distribution between the two scatterers provides the spatial information of a flexible molecule.

Article Title: Crystal structure of the complex of the interaction domains of Escherichia coli DnaB helicase and DnaC helicase loader: structural basis implying a distortion-accumulation mechanism for the DnaB ring opening caused by DnaC binding.
Article Snippet: Koji Nagata1,†, Akitoshi Okada1,†, Jun Ohtsuka1,†, Takatoshi Ohkuri2,‡, Yusuke Akama3, Yukari Sakiyama3, Erika Miyazaki3, Shoichiro Horita1, Tsutomu Katayama3,*, Tadashi Ueda2,* and Masaru Tanokura1,* 1 Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan 2 Department of Protein Structure, Function and Design, Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan 3 Department of Molecular Biology, Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan † These authors contributed equally to the paper as first authors.. ‡ Present Address: Takatoshi Ohkuri, Faculty of Pharmaceutical Sciences, Sojo University, Nishi-ku, Kumamoto, Kumamoto 860-0082, Japan * Corresponding authors: Tsutomu Katayama, Department of Molecular Biology, Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan.. Tel: +81 92 642 6641, Fax: +81 92 642 6646, email: katayama@phar.kyushu-u.ac.jp; Tadashi Ueda, Department of Protein Structure, Function and Design, Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan.

Article Title: Allopurinol and oxypurinol differ in their strength and mechanisms of inhibition of xanthine oxidoreductase.
Article Snippet: Parts of this work was performed at Spring-8 (Harima, Japan) under the Collaborative Research Program of Institute for Protein Research, Osaka University.

Article Title: Structural basis of Gip1 for cytosolic sequestration of G protein in wide-range chemotaxis
Article Snippet: Diffraction data were collected at BL26B1 and B2 of SPring-8 (Harima, Japan) at X-ray wavelengths of 1.0000 and 1.7000 Å for Form I and Form II, respectively.

Article Title: Organic thin film, and organic semiconductor device and organic transistor using same
Article Snippet: SPring-8 is a large synchrotron radiation facility which delivers the most powerful synchrotron radiation in the world and located in Harima Science Park City, Hyogo Prefecture.



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