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Your search keyword '"Naohiro Matsugaki"' showing total 3 results
Start Over Author "Naohiro Matsugaki" Publisher international union of crystallography
3 results on '"Naohiro Matsugaki"'

1. Long-wavelength native-SAD phasing: opportunities and challenges

Author

Shibom Basu, Vincent Olieric, Filip Leonarski, Naohiro Matsugaki, Yoshiaki Kawano, Tomizaki Takashi, Chia-Ying Huang, Yusuke Yamada, Laura Vera, Natacha Olieric, Jerome Basquin, Justyna A. Wojdyla, Oliver Bunk, Kay Diederichs, Masaki Yamamoto, and Meitian Wang

Subjects
single-wavelength anomalous dispersion, native-SAD phasing, Se/S-SAD, UV-laser cutting, crystal shaping, spherical crystals, absorption correction, anomalous scattering factor, structure determination, Crystallography, QD901-999
Abstract

Native single-wavelength anomalous dispersion (SAD) is an attractive experimental phasing technique as it exploits weak anomalous signals from intrinsic light scatterers (Z < 20). The anomalous signal of sulfur in particular, is enhanced at long wavelengths, however the absorption of diffracted X-rays owing to the crystal, the sample support and air affects the recorded intensities. Thereby, the optimal measurable anomalous signals primarily depend on the counterplay of the absorption and the anomalous scattering factor at a given X-ray wavelength. Here, the benefit of using a wavelength of 2.7 over 1.9 Å is demonstrated for native-SAD phasing on a 266 kDa multiprotein-ligand tubulin complex (T2R-TTL) and is applied in the structure determination of an 86 kDa helicase Sen1 protein at beamline BL-1A of the KEK Photon Factory, Japan. Furthermore, X-ray absorption at long wavelengths was controlled by shaping a lysozyme crystal into spheres of defined thicknesses using a deep-UV laser, and a systematic comparison between wavelengths of 2.7 and 3.3 Å is reported for native SAD. The potential of laser-shaping technology and other challenges for an optimized native-SAD experiment at wavelengths >3 Å are discussed.

Published
2019
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2. Protein crystallography beamline BL2S1 at the Aichi synchrotron

Author

Yusuke Yamada, Takayuki Nagae, Naohiro Matsugaki, Ayana Tomita, Masao Tabuchi, and Nobuhisa Watanabe

Subjects
0301 basic medicine, Diffraction, Nuclear and High Energy Physics, Materials science, 030106 microbiology, Analytical chemistry, 02 engineering and technology, Superconducting magnet, Crystallography, X-Ray, law.invention, 03 medical and health sciences, Optics, X-Ray Diffraction, law, protein crystallography, superbend beamline, Instrumentation, Monochromator, Radiation, Electromagnet, business.industry, Proteins, Beamlines, 021001 nanoscience & nanotechnology, Synchrotron, high pressure, Beamline, Goniometer, X-ray crystallography, 0210 nano-technology, business, Synchrotrons
Abstract

The protein crystallography beamline BL2S1 has been constructed on the 5 T superbend port of the AichiSR., The protein crystallography beamline BL2S1, constructed at one of the 5 T superconducting bending-magnet ports of the Aichi synchrotron, is available to users associated with academic and industrial organizations. The beamline is mainly intended for use in X-ray diffraction measurements of single-crystals of macromolecules such as proteins and nucleic acids. Diffraction measurements for crystals of other materials are also possible, such as inorganic and organic compounds. BL2S1 covers the energy range 7–17 keV (1.8–0.7 Å) with an asymmetric-cut curved single-crystal monochromator [Ge(111) or Ge(220)], and a platinum-coated Si mirror is used for vertical focusing and as a higher-order cutoff filter. The beamline is equipped with a single-axis goniometer, a CCD detector, and an open-flow cryogenic sample cooler. High-pressure protein crystallography with a diamond anvil cell can also be performed using this beamline.

Published
2017

3. Development of an X-ray HARP–FEA detector system for high-throughput protein crystallography

Author

Toshinobu Miyoshi, Norifumi Egami, Noriyuki Igarashi, Kenkichi Tanioka, Yusuke Yamada, Teruo Kawai, Kazuyuki Hyodo, Naohiro Matsugaki, Masakazu Namba, Misao Kubota, Soichi Wakatsuki, and Keiichi Hirano

Subjects
Nuclear and High Energy Physics, Diffraction Structural Biology, Materials science, Physics::Instrumentation and Detectors, Field emitter array, Crystallography, X-Ray, Sensitivity and Specificity, amorphous selenium, Crystal, Optics, protein crystallography, Instrumentation, Image resolution, Avalanche effect, imaging device, Radiation, business.industry, Detector, Proteins, semiconductor, avalanche multiplication, Frame rate, Amorphous solid, Semiconductor, HARP, business
Abstract

A new detector system for protein crystallography based on an X-ray HARP–FEA is presented., A new detector system for protein crystallography is now being developed based on an X-ray HARP–FEA (high-gain avalanche rushing amorphous photoconductor–field emitter array), which consists of an amorphous selenium membrane and a matrix field emitter array. The combination of the membrane avalanche effect with a single driven FEA has several advantages over currently available area detectors, including higher sensitivity, higher spatial resolution and a higher frame rate. Preliminary evaluation of the detector has been carried out and its effectiveness has been confirmed. Next, diffraction images were measured with continuous rotation of a protein crystal, and the images were compared with those measured by the existing CCD detector; the system successfully obtained high-spatial-resolution images. Using shutterless measurement, the total measurement time can be reduced significantly, making the method appropriate for high-throughput protein crystallography. The X-ray HARP–FEA detector is an attractive candidate for the next generation of X-ray area detectors.

Published
2008

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