Original Papers (only) <Year 1998>

Kumagai T., Muta K., Matoba Y., Kawano Y., Kamiya N., Dabies J., and Sugiyama M.: “Crystallization and preliminary X-ray diffraction studies of bleomyxin-binding protein form bleomycin-producing Streptomyces verticillus”, Acta Cryst. D54, 127-128 (1998).

Nakamura H., Saito K., Ito E., Tamura K., Tsuchiya T., Nishigaki K., Shiro Y., and Iizuka T.: “Identification of the hydrophobic amino acid residues required for heme assembly in the rhizobial oxygen sensor protein FixL”, Biochem. Biophys. Res. Commun. 247, 427-431 (1998).

Vibat C. R., Cecchini G., Nakamura K., Kita K., and Gennis R. B.: “Localization of histidine residues responsible for heme axial ligation in cytochrome b556 of complex II (succinate:ubiquinone oxidoreductase) in Escherichia coli”, Biochemistry 37, 4148-4159 (1998).

Okamoto N., Imai Y., Shoun H., and Shiro Y.: “Site-directed mutagenesis of the conserved threonine (Thr243) of the distal helix of fungal cytochrome P450nor”, Biochemistry 37, 8839-8847 (1998).

Singh U. P., Obayashi E., Takahashi S., Iizuka T., Shoun H., and Shiro Y.: “The effects of heme modification on reactivity, ligand binding properties and iron-coordination structures of cytochrome P450nor”, Biochim. Biophys. Acta 1384, 103-111 (1998).

Sugimoto T., Unno M., Shiro Y., Dou Yi., and Ikeda-Saito M.: “Myoglobin mutants giving the largest geminate yield in CO rebinding in nanosecond time domain”, Biophys. J. 75, 2188-2194 (1998).

Oda T., Makino K., Yamashita I., Namba K., and Maeda Y.: “Effect of the length and effective diameter of F-actin on the filament orientation in liquid crystalline sols measured by X-ray fiber diffraction”, Biophys. J. 75, 2672-2681 (1998).

Iwahara J., Kigawa T., Kitagawa K., Masumoto H., Okazaki T., and Yokoyama S.: “A helix-turn-helix structure unit in human centromere protein B (CENP-B)”, EMBO J. 17, 827-837 (1998).

Kigawa T., Endo M., Ito Y., Shirouzu M., Kikuchi A., and Yokoyama S.: “Solution structure of the Ras-binding domain of RGL”, FEBS Lett. 441, 413-418 (1998).

Kimoto M., Sakamoto K., Shirouzu M., Hirao I., and Yokoyama S.: “RNA aptamers that specifically bind to the Ras-binding domain of Raf-1”, FEBS Lett. 441, 322-326 (1998).

Obayashi E., Takahashi S., and Shiro Y.: “Electronic structure of reaction intermediate of cytochrome P450nor in its nitric oxide reduction”, J. Am. Chem. Soc. 120, 12964-12965 (1998).

Hiromasa Y., Aso Y., Mayanagi K., Inoue Y., Fujisawa T., Meno K., and Ueki T.: “Guanidine hydrochloride-induced changes of the E2 inner core of the Bacillus stearothermophilus pyruvate dehydrogenase complex”, J. Biochem. 123, 564-567 (1998).

Shirouzu M., Morinaka K., Koyama S., Hu C., Hori-Tamura N., Okada T., Kariya K., Kataoka T., Kikuchi A., and Yokoyama S.: “Interactions of the amino acid residue at position 31 of the c-Ha-Ras protein with Raf-1 and RalGDS”, J. Biol. Chem. 273, 7737-7742 (1998).

Yabuki T., Kigawa T., Dohmae N., Takio K., Terada T., Ito Y., Laue E., Cooper J., Kainosho M., and Yokoyama S.: “Dual amino acid-selective and site-directed stable-isotope labeling of the human c-Ha-Ras protein by cell-free synthesis”, J. Biomol. NMR 11, 295-306 (1998).

Ohata T., Konishi H., Kimura H., Furukawa Y., Tamasaku K., Nakatani T., Tanabe T., Matsumoto N., Ishii M., and Ishikawa T.: “SPring-8 beamline control system”, J. Synchrotron Rad. 5, 590-592 (1998).

Yamamoto M., Kumasaka T., Fujisawa T., and Ueki T.: “Trichromatic concept at SPring-8 RIKEN beamline I”, J. Synchrotron Rad. 5, 222-225 (1998). BL45XU

Goto S., Yabashi M., Ohashi H., Kimura H., Takeshita K., Uruga T., Mochizuki T., Kohmura Y., Kuroda M., Yamamoto M., Furukawa Y., Kamiya N., and Ishikawa T.: “Standard transport channels of X-ray beamlines at SPring-8”, J. Synchrotron Rad. 5, 1202-1205 (1998).

Kato M., and Fujisawa T.: “High-pressure solution X-ray scattering of protein using a hydrostatic cell with diamond window”, J. Synchrotron Rad. 5, 1282-1286 (1998).

Vassylyev D. G., Takeda S., Wakatsuki S., Maeda K., and Maeda Y.: “Crystal structure of troponin C in complex with N-terminal fragment of troponin I: The mechanism of how the inhibitory action of troponin I is released by Ca2+-binding to troponin C”, Mechanism of Work Production and Work Absorption in Muscle 157-167 (1998).

Nagashima S., Nakasako M., Dohmae N., Tsujimura M., Takio K., Odaka M., Yohda M., Kamiya N., and Endo I.: “Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms”, Nature Struct. Biol. 5, 347-351 (1998).

Yamamoto M., Kumasaka T., Uruga T., Kamiya N., Iwasaki H., and Ueki T.: “Evaluation of high spatial resolution imaging plate”, Nucl. Instrum. Methods Phys. Res. A 416, 314-318 (1998).

Kim J., Shirouzu M., Kataoka T., Bowtell D., and Yokoyama S.: “Activation of Ras and its downstream extracellular signal-regulated protein kinases by the CDC25 homology domain of mouse Son-of-sevenless 1 (mSos1)”, Oncogene 16, 2597-2607 (1998).

Vassylyev D. G., Takeda S., Wakatsuki S., Maeda K., and Maeda Y.: “Crystal structure of troponin C in complex with troponin I fragment at 2.3A resolution”, Proc. Natl. Acad. Sci. USA 95, 4847-4852 (1998).

Nishinaka T., Shinohara A., Ito Y., Yokoyama S., and Shibata T.: “Base-pair switching by interconversion of sugar puckers in DNA extended by proteins of RecA-family: A model for homology search in homologous genetic recombination”, Proc. Natl. Acad. Sci. USA 95, 11071-11076 (1998).

Nureki O., Vassylyev D., Tateno M., Shimada A., Nakama T., Fukai S., Konno M., Hendrickson T., Schimmel, P., and Yokoyama S.: “Enzyme structure with two catalytic sites for double-sieve selection of substrate”, Science 280, 578-582 (1998).

Tamura K., and Hasegawa T.: “Role of the terminal base-pair of acceptor stem and CCA sequence of tRNA in aminoacylation activity”, Viva Origino 26, 241-250 (1998).