Amino Acid Composition, Crystallization and Preliminary X-ray Diffraction Studies of Guanylonbonuclease from Streptomyces Aureofaciens
نویسندگان
چکیده
The amino acid composition and preparation of crystals for X ray diffraction analysis of guanylonbonuclease isolated from Streptomyces aureofa ciens is described. Single crystals have been grown from ammonium sulphate solutions. The crystals are orthorombic, space group P 2i2]2, cell dimmensions a = 6.47 nm, b = 7.89 nm, c = 3.93 nm. There are two molecules of a molecular weight of 10 600 in the asymmetric unit. The solvent content of the crystal is 50 %.
منابع مشابه
Evidence for the Essential Arginine and Histidine Residues in Catalytic Activity of Glucose 6-Phosphate Dehydrogenase from Streptomyces aureofaciens
Glucose 6-phosphate dehydrogenase (G6PD) was purified from Streptomyces aureofaciens and inactivated with butanedione and diethylpyrocarbonate. Incubation of the enzyme with butanedione resulted in a rapid activity loss (80%) within 5 min, followed by a slow phase using a molar ratio to enzyme concentration of 100. Fluorescence studies showed a conformational change in the butanedione-modified ...
متن کاملPurification, crystallization, and preliminary x-ray diffraction studies of the flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607.
The flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607 was purified by dye-ligand affinity chromatography. The protein was crystallized from solutions of high ionic strength, and one of the two crystal forms obtained has proven suitable for x-ray diffraction studies. Preliminary analysis showed that these crystals belong to the tetragonal space group 1422. The unit cell dimension...
متن کاملPurification, crystallization and preliminary X-ray diffraction studies of recombinant class A non-specific acid phosphatase of Salmonella typhimurium.
The phoN gene of Salmonella enterica sv. Typhimurium strain MD6001 was cloned in the multicopy plasmid pBluescript SK(-). The nucleotide sequence of the cloned gene differs from the corresponding S. typhimurium LT2 sequence at 23 residues, leading to 15 amino-acid differences, but was very close to the S. typhi phoN sequence (only three nucleotide and two amino-acid differences). The recombinan...
متن کاملExpression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter.
The Agrobacterium radiobacter CCRC 14924 N-carbamyl-D-amino-acid amidohydrolase, the enzyme used for production of D-amino acids, was overexpressed in Escherichia coli JM109. The expressed protein was crystallized by vapour diffusion using lithium sulfate as precipitant. It crystallizes in space group P21 with unit-cell parameters a = 69.8, b = 67.9 and c = 137.8 A and beta = 96.4 degrees. Ther...
متن کاملCrystallization and preliminary X-ray analysis of the aromatic prenyltransferase CloQ from the clorobiocin biosynthetic cluster of Streptomyces roseochromogenes
Crystals of recombinant CloQ (subunit MW = 35 626 Da; 324 amino acids), an aromatic prenyltransferase from Streptomyces roseochromogenes, were grown by vapour diffusion. The protein crystallizes in space group I4(1)22, with unit-cell parameters a = b = 135.19, c = 98.13 A. Native data from a single crystal were recorded to a resolution of 2.2 A in-house. Preliminary analysis of these data indic...
متن کامل