Shimizu H., Park S.-Y., Shiro Y., and Adachi S.: “X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution”, Acta Cryst. D58, 81-89 (2002). BL44B2

Nakano H., Uchiyama S., Yoshida T., Ohkubo T., Kato H., Yamagata Y., and Kobayashi Y.: “Crystallization and preliminary X-ray crystallographic studies of a mutant of ribosome recycling factor from Escherichia coli, Arg132Gly”, Acta Cryst. D58, 124-126 (2002).

Hibi T., Hisada H., Nakatsu T., Kato H., and Oda J.: “Escherichia coli ????-glutamylcysteine synthetase: modification, purification, crystallization and preliminary crystallographic analysis”, Acta Cryst. D58, 316-318 (2002).

Lee D.-S., Yamada A., Matsunaga I., Ichihara K., Adachi S., Park S.-Y., and Shiro Y.: “Crystallization and preliminary X-ray diffraction analysis of fatty-acid hydroxylase cytochrome P450BS? from Bacillus subtilis”, Acta Cryst. D58, 687-689 (2002).

Liu L., Nogi T., Kobayashi M., Nozawa T., and Miki K.: “Ultrahigh-resolution structure of high-potential iron-sulfur protein from Thermochromatium tepidum”, Acta Cryst., D58, 1085-1091 (2002). BL44B2

Nureki O., Shirouzu M., Hashimoto K., Ishitani R., Terada T., Tamakoshi M., Oshima T., Chijimatsu M., Takio K., Vassylyev D., Shibata T., Inoue Y., Kuramitsu S., and Yokoyama S.: “An enzyme with a deep trefoil knot for the active-site architecture” Acta Cryst. D58, 1129-1137 (2002).

Shimomura K., Sumiguchi-Agari K., Masui R., Kuramitsu S., and Fukuyama K.: “Overproduction, crystallization, and preliminary X-ray diffraction analysis of a quinone oxidoreductase from Thermus thermophilus HB8”, Acta Cryst. D58, 1365-1367 (2002). BL44B2

Vassylyeva M., Jookyung L., Sekine S., Oleg L., Kuramitsu S., Shibata T., Inoue Y., Sergei B., Vassylyev D., and Yokoyama S.: “Purification, crystallization and initial crystallographic analysis of RNA polymerase holoenzyme from Thermus thermophilus” Acta Cryst. D58, 1497-1500 (2002).

Shomura Y., Yoshida T., Maruyama T., Yohda M., and Miki K.: “Crystallization and preliminary X-ray characterization of archaeal group II chaperonin ? subunit from Thermococcus strain KS-1”, Acta Cryst., D58, 1830-1832 (2002). BL41XU/BL45PX

Yamamoto H., Yamauchi E., Taniguchi H., Ono T., and Miyamoto E.: “Phosphorylation of microtubule-associated protein tau by Ca2+/Calmodulin-activated protein kinase II in its tubulin binding sites.” Arch. Biochem. Biophys. 408, 255-262 (2002).

Kimura M., Furuichi M., Yamamoto M., Kumasaka T., Mizuno H., Miyano M., and Yamaguchi I.: “The flexible C-terminal region of Aspergillus terreus blasticidin S deaminase: Identification of its functional roles with deletion enzymes”, Biochem. Biophys. Res. Commun. 290, 421-426 (2002).

Matsunaga I., Yamada A., Lee D.-S., Obayashi E., Fujiwara N., Kobayashi K., Ogura H., and Shiro Y.: “Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: Kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy”, Biochemistry 41, 1886-1892 (2002).

Noguchi T., and Sugiura M.: “Flash-induced FTIR difference spectra of the water oxidizing complex in moderately hydrated photosystem II core films: Effect of hydration extent on S-state transitions”, Biochemistry 41, 2322-2330 (2002).

Shimizu T., Nakatsu T., Miyairi K., Okuno T., and Kato H.: “Active-site architecture of endopolygalacturonase I from Stereum purpureum revealed by crystal structures in native and ligand-bound forms at atomic resolution”, Biochemistry 41, 6651-6659 (2002).

Tanaka M., Machida Y., Nishikawa Y., Akagi T., Morishima I., Hashikawa T., Fujisawa T., and Nukina N.: “The effects of aggregation-inducing motifs on amyloid formation of model proteins related to neurodegenerative diseases”, Biochemistry 41, 10277-10286 (2002). BL45SAXS

Fujisawa T., Kato M., Taguchi Y., Stanley H. E., and Ludwig H.: “The small angle X-ray scattering from proteins under pressure”, Biological Systems Under Extreme Conditions: Structure and Function, 121-138 (2002).

Iwamoto H., Nishikawa Y., Wakayama J., and Fujisawa T.: “Direct X-ray observation of a single hexagonal myofilament lattice in native myofibrils of striated muscle”, Biophys. J. 83, 1074-1081 (2002).
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Krieger I., Kostyukova A., Yamashita A., Nitanai Y., and Maeda Y.: “Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping”, Biophys. J. 83, 2716-2725 (2002). BL44B2

Tahirov T. H., Sato K., Ichikawa E., Sasaki M., Bungo T., Shiina M., Kimura K., Takata S., Fujikawa A., Morii H., Kumasaka T., Yamamoto M., Ishii S., and Ogata K.: “Mechanism of c-Myb-C/EBP ? cooperation from separated sites on a promoter”, Cell 108, 57-70 (2002). BL45XU

Ogiso H., Ishitani R., Nureki O., Fukai S., Yamanaka., Kim J-H., Saito K., Sakamoto A., Inoue M., Shirouzu M., and Yokoyama S.: “Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains” Cell 110, 775-787 (2002).

Nureki O., Fukai S., Sekine S., Shimada A., Terada T., Nakama T., Shirouzu M., Vassylyev D.G., and Yokoyama S.: “Structural basis for amino acid and tRNA recognition by Class I aminoacyl-tRNA synthetases” Cold Spring Harbor Laboratory Symposia on Quantitative Biology LXVI, 167-173 (2002).

Kimoto M., Shirouzu M., Mizutani S., Koide H., Kaziro Y., Hirao I., and Yokoyama S.: “Anti-(Raf-1) RNA aptamers that inhibit Ras-induced Raf-1 activation”, Eur. J. Biochem. 269, 697-704 (2002).

Liu L., Iwata K., Yohda M., and Miki K.: “Structural insight into gene duplication, gene fusion and domain swapping in the evolution of PLP-independent amino acid racemases”, FEBS Lett., 528, 114-118 (2002). BL44B2

Satoh T., Itoga A., Isogai Y., Kurihara M., Yamada S., Natori M., Suzuki N., Suruga K., Kawachi R., Arahira M., Nishio T., Fukazawa C., and Oku T.: “Increasing the conformational stability by replacement of heme axial ligand in c-type cytochrome” FEBS Lett. 531, 543-547 (2002).

Sano K., Maeda K., Oki M., and Maeda Y.: “Enhancement of protein expression in insect cells by a lobster tropomyosin cDNA leader sequence” FEBS Lett. 532, 143-146 (2002).

Nameki N., Someya T., Hosoi H., Suzuki S., Hatanaka H., Fujii M., Terada T., Shirouzu M., Inoue Y., Shibata T., Kuramitsu S., Yokoyama S., and Kawai G.: “Solution structure of a tmRNA-binding protein, SmpB, from Thermus thermophilus” FEBS Lett. 535, 94-100 (2002).

Hori H., Suzuki T., Sugawara K., Inoue Y., Shibata T., Kuramitsu S., Yokoyama S., Oshima T., and Watanabe K.: “Identification and characterization of tRNA (Gm18) methyltransferase from Thermus thermophilus HB8: domain structure and conserved amino acid sequence motifs” Genes Cells 7, 259-272 (2002).

Ogata H., Mizoguchi Y., Mizuno N., Miki K., Adachi S., Yasuoka N., Yagi T., Yamauchi O., Hirota S., and Higuchi Y.: “Structural studies of the carbon monoxide complex of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F: Suggestion for the initial activation site for dihydrogen”, J. Am. Chem. Soc., 39, 11628-11635 (2002). BL44B2

Sakai K., Matsui Y., Kohyama T., Shiro Y., and Adachi S.: “Optical monitoring of freeze-trapped reaction intermediates in protein crystals: a microspectro-photometer for cryogenic protein crystallography”, J. Appl. Crystallogr. 35, 270-273 (2002).

Hai H., Sano K., Maeda K., Maeda Y., and Miki M.: “Ca2+- and S1-induced conformational changes of reconstituted skeletal muscle thin filaments observed by fluorescence energy transfer spectroscopy: Structural evidence for three states of thin filament”, J. Biochem. 131, 407-418 (2002).

Kuwahara H., Yamasaki T., Hatakeyama T., Aoyagi H., and Fujisawa T.: “Oligomerization process of the hemolytic lectin CEL-III purified from a sea cucumber, Cucumaria echinata”, J. Biochem. 131, 751-756 (2002). BL45SAXS

Kimura C., Maeda K., Maeda Y., and Miki M.: “Ca2+- and S1-induced movement of troponin T on reconstituted skeletal muscle thin filaments observed by fluorescence energy transfer spectroscopy1”, J. Biochem. 132, 93-102 (2002).

Kimura C., Maeda K., Hai H., and Miki M.: “Ca2+ -and S1-induced movement of troponin T on mutant thin filaments reconstituted with functionally deficient mutant tropomyosin”, J. Biochem. 132, 345-352 (2002).

Omi R., Mizuguchi H., Goto M., Miyahara I., Hayashi H., Kagamiyama H., and Hirotsu K.: “Structure of Imidazole Glycerol Phosphate Synthase from Thermus thermophilus HB8: Open-Closed Conformational Change and Ammonia Tunneling1” J. Biochem. 132, 759-765 (2002).

Kurumizaka H., Ikawa S., Nakada M., Enomoto R., Kagawa W., Kinebuchi T., Yamazoe M., Yokoyama S., and Shibata T.: “Homologous pairing and ring and filament structure formation activities of the human Xrcc2?Rad51D complex”, J. Biol. Chem. 277, 14315-14320 (2002).

Goto M., Nakajima Y., and Hirotsu K.: “Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8: Structural basis for the catalytic action”, J. Biol. Chem. 277, 15890-15896 (2002).
BL41XU/BL44B2/BL45XU.

Kikuchi J., Iwahara J., Kigawa T., Murakami Y., Okazaki T., and Yokoyama S.: “Solution structure of the two DNA-binding domains in Shizosaccharomyces pombe Abp1 protein by a combination of dipolar coupling and diffusion anisotropy restraints” J. Biomol. NMR 22, 333-347 (2002).

Hayashi T., Matsuo T., Hitomi Y., Okawa K., Shiro Y., Iizuka T., Hisaeda Y., and Ogoshi H.: “Contribution of heme-propionate side chains to structure and function of myoglobin: Chemical approach by artificially created prosthetic groups” J. Inorg. Biochem. 91, 94-100 (2002).

Park S.-Y., Yamane K., Adachi S., Shiro Y., Weiss K. E., Maves S. A., and Sligar S. G.: “Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: High resolution structural origin of its thermostability and functional properties” J. Inorg. Biochem. 91, 491-501 (2002). BL44B2

Iwamoto H., Oiwa K., Suzuki T., and Fujisawa T.: “States of thin filament regulatory proteins as revealed by combined cross-linking/X-ray diffraction techniques”, J. Mol. Biol. 317, 707-720 (2002). BL45SAXS

Ishitani R., Nureki O., Fukai S., Kijimoto T., Nameki N., Watanabe M., Kondo H., Sekine M., Okada N., Nishimura S., and Yokoyama S.: “Crystal structure of Archaeosine tRNA-guanine Transglycosylase” J. Mol. Biol. 318, 665-677 (2002).

Furukawa Y., Imada K., Vonderviszt F., Matsunami H., Sano K., Kutukake K., and Namba K.: “Interaction between bacterial flagellar axial proteins in their monomeric state in solution” J. Mol. Biol. 318, 889-900 (2002).

Irie K., Nakatsu T., Mitsuoka K., Miyazawa A., Sobue K., Hiroaki Y., Doi T., Fujiyoshi Y., and Kato H.: “Crystal structure of the homer 1 family conserved region reveals the interaction between the EVH1 domain and own proline-rich motif”, J. Mol. Biol. 318, 1117-1126 (2002).

Liu L., Iwata K., Kita A., Kawarabayasi Y., Yohda M., and Miki K.: “Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implication for molecular mechanism of PLP-independent racemization”, J. Mol. Biol., 319, 479-489 (2002). BL44B2

Unwin N., Miyazawa A., Li J., and Fujiyoshi Y.: “Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the ? subunits”, J. Mol. Biol. 319, 1165-1176 (2002).

Fukushima K., Kikuchi J., Koshiba S., Kuroda Y., and Yokoyama S.: “Solution structure of the C-terminal domain of DEF45/ICAD. A structural basis for the regulation of apoptotic DNA fragmentation” J. Mol. Biol. 321, 317-327 (2002).

Ohyama A., Hosaka K., Komiya Y., Akagawa K., Yamauchi E., Taniguchi H., Sasagawa N., Kumakura K., Mochida S., Yamauchi T., and Igarashi M.: “Regulation of exocytosis through Ca2+/ATP-dependent binding of autophosphorylated Ca2+/Calmodulin-activated protein kinase II to syntaxin 1A ” J. Neurosci. 22, 3342-3351 (2002).

Hasegawa K., Ono T., and Noguchi T.: “Ab initio density functional theory calculations and vibrational analysis of zinc-bound 4-methylimidazole as a model of a histidine ligand in metalloenzymes”, J. Phys. Chem. A 106, 3377-3390 (2002).

Hendrickson T. L., Nomanbhoy T. K., DeCrecy-Lagard V., Fukai S., Nureki O., Yokoyama S., and Schimmel P.: “Mutational separation of two pathways for editing by a class I tRNA synthetase” Mol. Cell 9, 353-362 (2002).

Kagawa W., Kurumizaka H., Ishitani R., Fukai S., Nureki O., Shibata T., and Yokoyama S.: “Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form” Mol. Cell 10, 359-371 (2002).

Vassylyev D., Sekine S, Oleg L., Jookyung L., Vassylyeva M., Sergei B., and Yokoyama S.: “Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution” Nature 417, 712-719 (2002).

Tahir T. H., Temiakov D., Anikin M., Patlan V., McAllister W. T., Vassylyev D., and Yokoyama S.: “Structure of a T7 RNA polymerase elongation complex at 2.9 A resolution” Nature 420, 43-50 (2002).

Kita A., Matsunaga S., Takai A., Kataiwa H., Wakimoto T., Fusetani N., Isobe M., and Miki K.: “Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1” Structure 10, 715-724 (2002).

Hirao I., Ohtsuki T., Fujiwara T., Mitsui T., Yokogawa T., Okuni T., Nakayama H., Takio K., Yabuki T., and Kigawa T.: “An unnatural base pair for incorporating amino acid analogs into proteins”, Nature Biotechnol. 20, 177-182 (2002).

Terada T., Nureki O., Ishitani R., Ambrogelly A., Ibba M., Soll D., and Yokoyama S.: “Functional convergence of two lysyl-tRNA synthetases with unrelated topologies” Nat. Struct. Biol. 9, 257-262 (2002).

Hardingham G., Fukunaga Y., and Bading H.: “Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways”, Nature Neuroscience 5, 405-414 (2002).

Sakamoto K., Hayashi A., Sakamoto A., Kiga D., Nakayama H., Soma A., Kobayashi T., Kitabatake M., Takio K., Saito K., Shirouzu M., Hirao I., and Yokoyama S.: “Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells” Nucleic Acids Res. 30, 4692-4699 (2002).

Yamamoto A., and Yamaguchi I.: “Profilometry of sloped plane surfaces by wavelength scanning interferometry”, Opt. Rev. 9, 112-121 (2002).

Tohri A., Suzuki T., Okuyama S., Kamino K., Motoki A., Hirano M., Ohta H., Shen J.R., Yamamoto Y., and Enami I.: “Comparison of the structure of the extrinsic 33 kDA protein from different organisms” Plant Cell Physiol. 43, 429-439 (2002).

Akiyama S., Takahashi S., Kimura T., Ishimori K., Morishima I., Nishikawa Y., and Fujisawa T.: “Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering”, Proc. Natl. Acad. Sci. USA 99, 1329-1334 (2002). BL45SAXS

Yamagata A., Masui R., Kakuta Y., Fukuyama K.: “The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity”, Proc. Natl. Acad. Sci. USA 99, 5908-5912 (2002). BL41XU

Isogai Y., Ota M., Ishii A., Ishida M., and Nishikawa K.: “Identification of amino acids involved in protein structural uniqueness: implication for de novo protein design” Protein Eng. 15, 555-560 (2002).

Kita A., Matsunaga S., Takai A., Kataiwa H., Wakimoto T., Fusetani N., Isobe M., and Miki K.: “Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1”, Structure, 10, 715-724 (2002). BL44B2

Fujisawa T., Nisikawa Y., Inoko Y., and Hayashi R.: “The use of a small-angle X-ray scattering technique with a third generation synchrotron X-ray source in high-pressure biochemistry”, Trends in High Pressure Bioscience and Biotechnology , 615-620 (2002). BL45SAXS