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The MinD protein from the hyperthermophilic archaeon Pyrococcus horikoshii: crystallization and preliminary X-ray analysis. 2001

N Sakai, and H Itou, and N Watanabe, and M Yao, and I Tanaka
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.

MinD is one of the proteins regulating cell division. MinD from Escherichia coli has been designated as a type of motor protein which has an ATPase activity. This paper deals with the first crystallization and preliminary crystallographic analysis of recombinant MinD from Pyrococcus horikoshii (molecular weight 26.3 kDa) expressed in E. coli. Crystals of MinD were obtained by the hanging-drop vapour-diffusion method. MinD crystals belong to space group P2(1)3, with unit-cell parameters a = b = c = 98.5 A, and diffract to 3.0 A resolution. The asymmetric units each contain one molecule of MinD, giving a crystal volume per protein mass (V(M)) of 3.0 A(3) Da(-1) and a solvent content of 59.0%.

UI MeSH Term Description Entries
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D003460 Crystallization The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Crystalline Polymorphs,Polymorphism, Crystallization,Crystal Growth,Polymorphic Crystals,Crystal, Polymorphic,Crystalline Polymorph,Crystallization Polymorphism,Crystallization Polymorphisms,Crystals, Polymorphic,Growth, Crystal,Polymorph, Crystalline,Polymorphic Crystal,Polymorphisms, Crystallization,Polymorphs, Crystalline
D000251 Adenosine Triphosphatases A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA. ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D018360 Crystallography, X-Ray The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) X-Ray Crystallography,Crystallography, X Ray,Crystallography, Xray,X Ray Crystallography,Xray Crystallography,Crystallographies, X Ray,X Ray Crystallographies
D019711 Pyrococcus A genus of strictly anaerobic ultrathermophilic archaea, in the family THERMOCOCCACEAE, occurring in heated seawaters. They exhibit heterotrophic growth at an optimum temperature of 100 degrees C.
D019843 Archaeal Proteins Proteins found in any species of archaeon. Archaeal Gene Products,Archaeal Gene Proteins,Archaeal Peptides,Gene Products, Archaeal,Gene Proteins, Archaeal
D029968 Escherichia coli Proteins Proteins obtained from ESCHERICHIA COLI. E coli Proteins

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