Kunio Miki mostly deals with Stereochemistry, Biochemistry, Crystallography, Protein structure and Crystal structure. His study in Stereochemistry is interdisciplinary in nature, drawing from both Amino acid, Hydrolase, DNA, Active site and Peptide sequence. His Crystallography research is multidisciplinary, relying on both Aspartic acid, Flavin group and Bacteriochlorophyll.
His Protein structure research incorporates elements of Periplasmic space, Protein subunit, Ring and Binding site. His studies deal with areas such as Ligand, ATP synthase and Fucose as well as Binding site. His research in Crystal structure intersects with topics in Ion, Photochemistry, Molecule and Thermococcus.
His primary areas of investigation include Crystallography, Stereochemistry, Crystal structure, Biochemistry and Molecule. He has researched Crystallography in several fields, including X-ray crystallography and Crystallization. The Crystallization study combines topics in areas such as Orthorhombic crystal system, Space group and Ammonium sulfate.
His Stereochemistry study combines topics in areas such as Protein subunit, Active site, Dimer, Thermus thermophilus and Protein structure. His work in Crystal structure tackles topics such as Thermococcus which are related to areas like Chaperonin. His Biochemistry study is mostly concerned with Enzyme, Thermococcus kodakarensis, Binding site, Peptide sequence and Mutant.
Biochemistry, Crystallography, Crystal structure, Stereochemistry and Thermococcus kodakarensis are his primary areas of study. His Crystallography study also includes fields such as
His Biophysics research focuses on subjects like Protein folding, which are linked to Peptide sequence. The various areas that Kunio Miki examines in his Stereochemistry study include Selectivity, Ligand and Heme. His work deals with themes such as Hydrogenase, Protease, Thermococcales, Thermococcus and Active site, which intersect with Thermococcus kodakarensis.
Kunio Miki mainly investigates Stereochemistry, Crystallography, Thermococcus kodakarensis, Biochemistry and Hydrogenase. Kunio Miki combines subjects such as Chaperone activity, Ligand, Active site, Protein structure and Binding site with his study of Stereochemistry. He mostly deals with Crystal structure in his studies of Crystallography.
His research investigates the connection between Crystal structure and topics such as Sulfolobus tokodaii that intersect with problems in Self-assembly. His biological study spans a wide range of topics, including Isomerase, Conformational change and Thermococcus. His Hydrogenase research incorporates themes from ATPase, GTPase, Cysteine and Ternary complex.
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Structural genomics projects in Japan.
Shigeyuki Yokoyama;Hiroshi Hirota;Takanori Kigawa;Takashi Yabuki.
Nature Structural & Molecular Biology (2000)
Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4 A resolution.
Yoshiki Higuchi;Hideaki Ogata;Kunio Miki;Noritake Yasuoka.
Crystal structure of DNA photolyase from Anacystis nidulans.
T Tamada;T Tamada;K Kitadokoro;Y Higuchi;K Inaka.
Nature Structural & Molecular Biology (1997)
Structure of the LH1–RC complex from Thermochromatium tepidum at 3.0 Å
Satomi Niwa;Long Jiang Yu;Kazuki Takeda;Yu Hirano.
Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability and electron transfer
Terukazu Nogi;Insan Fathir;Masayuki Kobayashi;Tsunenori Nozawa.
Proceedings of the National Academy of Sciences of the United States of America (2000)
Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase
Masahiro Fujihashi;Yuan-Wei Zhang;Yoshiki Higuchi;Xiao-Yuan Li.
Proceedings of the National Academy of Sciences of the United States of America (2001)
Structure of a Cyanobacterial BLUF Protein, Tll0078, Containing a Novel FAD-binding Blue Light Sensor Domain
Akiko Kita;Koji Okajima;Yukio Morimoto;Masahiko Ikeuchi.
Journal of Molecular Biology (2005)
An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2
Akiko Kita;Shin-ichi Kita;Ikuhide Fujisawa;Koji Inaka.
Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA
Satoshi Watanabe;Akiko Kita;Kazuo Kobayashi;Kunio Miki.
Proceedings of the National Academy of Sciences of the United States of America (2008)
Crystal structures of bacterial lipoprotein localization factors, LolA and LolB
Kazuki Takeda;Hideyuki Miyatake;Naoko Yokota;Shin‐ichi Matsuyama.
The EMBO Journal (2003)
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