The three-dimensional structure of mitochondrial aspartate aminotransferase at 4.5 A resolution.

[1]  A. McPherson,et al.  The growth and preliminary investigation of protein and nucleic acid crystals for X-ray diffraction analysis. , 2006, Methods of biochemical analysis.

[2]  M. Solioz,et al.  Biogenesis of the cytochrome bc1 complex of yeast mitochondria. A precursor form of the cytoplasmically made subunit V. , 1979, The Journal of biological chemistry.

[3]  P. Christen,et al.  Mitochondrial and cytosolic aspartate aminotransferase from chicken: activity toward aromatic amino acids. , 1978, Biochemical and biophysical research communications.

[4]  B. Vainshtein,et al.  Three-dimensional structure at 5 A resolution of cytosolic aspartate transaminase from chicken heart. , 1978, Journal of molecular biology.

[5]  P. Christen,et al.  Comparison of the evolution rates of cytosolic and mitochondrial aspartate aminotransferase , 1978, Nature.

[6]  D. Metzler,et al.  Crystalline enzyme.substrate complexes of asparate aminotransferase. , 1978, The Journal of biological chemistry.

[7]  G. Eichele,et al.  Catalytic activity in crystals of mitochondrial aspartate aminotransferase as detected by microspectrophotometry. , 1978, The Journal of biological chemistry.

[8]  P. Christen,et al.  Syncatalytic conformational changes in mitochondrial aspartate aminotransferases. Evidence from modification and demodification of Cys 166 in the enzyme from chicken and pig. , 1978, The Journal of biological chemistry.

[9]  G. Petsko,et al.  On the protein crystal chemistry of chloroplatinite ions: general principles and interactions with triose phosphate isomerase. , 1978, Journal of molecular biology.

[10]  P. Highfield,et al.  Synthesis and transport of the small subunit of chloroplast ribulose bisphosphate carboxylase , 1978, Nature.

[11]  P. Christen,et al.  Cytosolic aspartate aminotransferase. Studies on subunit interactions with the apo/holo hybrid dimer. , 1978, Biochimica et biophysica acta.

[12]  F. Bossa,et al.  The structure of mitochrondrial aspartate aminotransferase from pig heart and comparison with that of the cytoplasmic isozyme , 1977, FEBS letters.

[13]  G. Eichele,et al.  Isolation, crystallization and preliminary crystallographic data of aspartate aminotransferase from chicken heart mitochondria. , 1977, Journal of molecular biology.

[14]  P. Christen,et al.  Aspartate aminotransferase. Determination of the active site occupancy pattern indicates independent transamination of the two subunits. , 1977, The Journal of biological chemistry.

[15]  H. Kagamiyama,et al.  The complete amino acid seqeunce of mitochondrial asparatate aminotransferase from pig heart. , 1977, Journal of biochemistry.

[16]  D. Metzler,et al.  Preliminary crystallographic study of aspartate: 2-oxoglutarate aminotransferase from pig heart. , 1977, Journal of molecular biology.

[17]  C. Wright,et al.  The crystal structure of wheat germ agglutinin at 2-2 A resolution. , 1977, Journal of molecular biology.

[18]  P. Christen,et al.  Interspecies comparison of cytosolic and mitochondrial aspartate aminotransferases. Evidence for a more conservative evolution of the mitochondrial isoenzyme. , 1977, The Journal of biological chemistry.

[19]  A. Klug,et al.  Crystallographic refinement of yeast phenylalanine transfer RNA at 2-5A resolution. , 1976, Journal of molecular biology.

[20]  M. Martinez‐Carrion,et al.  Itemizing enzyme ligand interactions in native and and half-active hybrid aspartate transaminase to probe site-site relationships. , 1976, Biochemistry.

[21]  G. Bricogne,et al.  Methods and programs for direct‐space exploitation of geometric redundancies , 1976 .

[22]  T. Steitz,et al.  High resolution x-ray structure of yeast hexokinase, an allosteric protein exhibiting a non-symmetric arrangement of subunits. , 1976, Journal of molecular biology.

[23]  M. Martinez‐Carrion,et al.  Hybridization of glutamate aspartate transaminase. Investigation of subunit interaction. , 1975, Biochemistry.

[24]  P. Fasella,et al.  The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues. , 1975, The Biochemical journal.

[25]  Y. Lee,et al.  Mitochondrial aspartate aminotransferase-independent function of the catalytic binding sites. , 1975, The Journal of biological chemistry.

[26]  P. Christen,et al.  The apo-holo hybrid of cytosolic aspartate aminotransferase, preparation and studies on subunit interactions. , 1974, Biochemical and biophysical research communications.

[27]  P. Christen,et al.  Cytoplasmic aspartate aminotransferase: syncatalytic sulfhydryl group modification. , 1973, The Journal of biological chemistry.

[28]  Y. Morino,et al.  Evidence for the presence of a distinct subsite for binding the distal carboxyl group of dicarboxylate substrates and its role in the catalytic activity of aspartate aminotransferase. , 1972, Biochemical and biophysical research communications.

[29]  E Shrawder,et al.  Evidence of phenylalanine transaminase activity in the isoenzymes of aspartate transaminase. , 1972, The Journal of biological chemistry.

[30]  R. Scandurra,et al.  Mitochondrial aspartate aminotransferase from beef kidney. , 1972, European journal of biochemistry.

[31]  J. Miller,et al.  Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase. , 1971, The Journal of biological chemistry.

[32]  D. Tiemeier,et al.  Conformational properties of the isoenzymes of aspartate transaminase and the enzyme-substrate complexes. , 1970, Biochemistry.

[33]  R. Khomutov,et al.  The synthesis and properties of phosphopyridoxyl amino acids. , 1969, Biochemical and biophysical research communications.

[34]  M. Rossmann,et al.  Low resolution study of crystalline L-lactate dehydrogenase. , 1969, Journal of molecular biology.

[35]  F. S. Mathews,et al.  A semi-empirical method of absorption correction , 1968 .

[36]  M. Ikawa Synthesis and properties of some N-pyridoxyl-L-amino acids and N-(5-phosphopyridoxyl)-L-amino acids. , 1967, Archives of biochemistry and biophysics.

[37]  T. I. Diamondstone Assay of tyrosine transaminase activity by conversion of p-hydroxyphenylpyruvate to p-hydroxybenzaldehyde☆ , 1966 .

[38]  J. Waser,et al.  Least-squares refinement with subsidiary conditions , 1963 .

[39]  F. Crick,et al.  The treatment of errors in the isomorphous replacement method , 1959 .

[40]  E. Lin,et al.  The assay of aromatic amino acid transaminations and keto acid oxidation by the enol borate-tautomerase method. , 1958, The Journal of biological chemistry.

[41]  P. S. Chen,et al.  Microdetermination of Phosphorus , 1956 .

[42]  Y. Ovchinnikov,et al.  The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heart , 1973, FEBS letters.