What is he best known for?
The fields of study he is best known for:
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 most cited work include:
- Structural genomics projects in Japan. (279 citations)
- 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. (238 citations)
- Crystal structure of DNA photolyase from Anacystis nidulans. (180 citations)
What are the main themes of his work throughout his whole career to date?
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.
He most often published in these fields:
- Crystallography (38.42%)
- Stereochemistry (35.56%)
- Crystal structure (33.89%)
What were the highlights of his more recent work (between 2010-2021)?
- Biochemistry (26.49%)
- Crystallography (38.42%)
- Crystal structure (33.89%)
In recent papers he was focusing on the following fields of study:
Biochemistry, Crystallography, Crystal structure, Stereochemistry and Thermococcus kodakarensis are his primary areas of study.
His Crystallography study also includes fields such as
- Protein structure together with Molecule,
- Photosynthetic bacteria which is related to area like Electron transfer.
His Crystal structure study combines topics from a wide range of disciplines, such as Biophysics, Chaperone, Dimer, RC complex and Catalysis.
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.
Between 2010 and 2021, his most popular works were:
- Structure of the LH1–RC complex from Thermochromatium tepidum at 3.0 Å (147 citations)
- Charge-density analysis of an iron–sulfur protein at an ultra-high resolution of 0.48 Å (50 citations)
- Nonequivalence Observed for the 16-Meric Structure of a Small Heat Shock Protein, SpHsp16.0, from Schizosaccharomyces pombe (46 citations)
In his most recent research, the most cited papers focused on:
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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