Original Papers (only)< Year 1998 >Kumagai T., Muta K., Matoba Y., Kawano Y., Kamiya N., Dabies J., and Sugiyama M.: “Crystallizationand 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:ubiquinoneoxidoreductase) 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 Maéda Y.: “Effect of the length and effective diameterof 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 theRas-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 bindto 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.: “Guanidinehydrochloride-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., andYokoyama 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., KurodaM., 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 cellwith diamond window”, J. Synchrotron Rad. 5, 1282-1286 (1998).
Vassylyev D. G., Takeda S., Wakatsuki S., Maeda K., and Maéda Y.: “Crystal structure of troponin C incomplex 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 inMuscle 157-167 (1998).
Nagashima S., Nakasako M., Dohmae N., Tsujimura M., Takio K., Odaka M., Yohda M., Kamiya N., andEndo I.: “Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms”, NatureStruct. 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 Maéda Y.: “Crystal structure of troponin C incomplex with troponin I fragment at 2.3Å 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 interconversionof sugar puckers in DNA extended by proteins of RecA-family: A model for homology search inhomologous 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 ofsubstrate”, Science 280, 578-582 (1998).

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