Literature DB >> 15263482

Trichromatic Concept at SPring-8 RIKEN Beamline I.

M Yamamoto1, T Kumasaka, T Fujisawa, T Ueki.   

Abstract

SPring-8 RIKEN beamline I has been designed and developed for structural biology research by the Institute of Physical and Chemical Research (RIKEN). The beamline consists of two experimental stations for protein crystallography and small-angle X-ray scattering. Both types of experiments can be carried out simultaneously, with dichromatic synchrotron radiation emitted from two coaxial undulators with vertical polarization. The branched beams are generated by a transparent diamond crystal. With synchrotron radiation, the multiple-wavelength anomalous-dispersion (MAD) method, which gives phases from a single anomalous scatterer, has been developed. Anomalous scattering contributes a small proportion of the diffraction intensity so that the accuracy of intensity data is important. The protein crystallography branch of RIKEN beamline I has been designed based on a 'trichromatic concept' to optimize MAD data collection. This concept requires the quasi-simultaneous collection, by use of a 'trichromator', of three intensity data sets at three different wavelengths from a single protein crystal without changing any settings. The main feature of the concept is the minimization of systematic errors in the measurement of anomalous diffraction for the MAD method. Initial commissioning of the beamline has provided three different monochromated undulator beams, which were successfully observed on the phosphor screen located at the near end of the trichromator.

Entities:  

Year:  1998        PMID: 15263482     DOI: 10.1107/S0909049597014738

Source DB:  PubMed          Journal:  J Synchrotron Radiat        ISSN: 0909-0495            Impact factor:   2.616


  7 in total

1.  Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch.

Authors:  T Toyoda; O F Tin; K Ito; T Fujiwara; T Kumasaka; M Yamamoto; M B Garber; Y Nakamura
Journal:  RNA       Date:  2000-10       Impact factor: 4.942

2.  Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8.

Authors:  M Sugahara; T Mikawa; T Kumasaka; M Yamamoto; R Kato; K Fukuyama; Y Inoue; S Kuramitsu
Journal:  EMBO J       Date:  2000-08-01       Impact factor: 11.598

3.  Structure of P-protein of the glycine cleavage system: implications for nonketotic hyperglycinemia.

Authors:  Tadashi Nakai; Noriko Nakagawa; Nobuko Maoka; Ryoji Masui; Seiki Kuramitsu; Nobuo Kamiya
Journal:  EMBO J       Date:  2005-03-24       Impact factor: 11.598

4.  Crystal structure of a novel polyisoprenoid-binding protein from Thermus thermophilus HB8.

Authors:  Noriko Handa; Takaho Terada; Yukiko Doi-Katayama; Hiroshi Hirota; Jeremy R H Tame; Sam-Yong Park; Seiki Kuramitsu; Mikako Shirouzu; Shigeyuki Yokoyama
Journal:  Protein Sci       Date:  2005-03-01       Impact factor: 6.725

5.  Crystal structure of the histidine-containing phosphotransfer protein ZmHP2 from maize.

Authors:  Hajime Sugawara; Yoshiaki Kawano; Tomomitsu Hatakeyama; Tomoyuki Yamaya; Nobuo Kamiya; Hitoshi Sakakibara
Journal:  Protein Sci       Date:  2004-12-02       Impact factor: 6.725

6.  Structural insight into the reaction mechanism and evolution of cytokinin biosynthesis.

Authors:  Hajime Sugawara; Nanae Ueda; Mikiko Kojima; Nobue Makita; Tomoyuki Yamaya; Hitoshi Sakakibara
Journal:  Proc Natl Acad Sci U S A       Date:  2008-02-07       Impact factor: 11.205

7.  Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase.

Authors:  Takashi Kumasaka; Kosuke Aritake; Hideo Ago; Daisuke Irikura; Toshiharu Tsurumura; Masaki Yamamoto; Masashi Miyano; Yoshihiro Urade; Osamu Hayaishi
Journal:  J Biol Chem       Date:  2009-06-22       Impact factor: 5.157

  7 in total

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