Crystallization and preliminary crystallographic investigations of rhodanese from Azotobacter vinelandii.
The rhdA gene identified in Azotobacter vinelandii codes for a protein, RhdA, which displays rhodanese (thiosulfate-cyanide sulfurtransferase) activity. RhdA was overexpressed and purified to homogeneity. The protein crystallized in the orthorhombic space group P2(1)2(1)2 with unit-cell parameters a = 44.4, b = 150.8, c = 53.8 A; on a synchrotron source the diffraction patterns could be collected to a resolution limit of 1.8 A. Evaluation of the crystal density indicates that the crystal lattice accommodates one molecule per asymmetric unit and that the solvent content is 59% of the total volume.
Bordo
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D
Advanced Biotechnology Center - IST and University of Genova - INFM, Largo R. Benzi 10, 16132 Genova, Italy. bordo@ermes.cba.unige.it
Colnaghi
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R
Deriu
D
D
Carpen
A
A
Storici
P
P
Pagani
S
S
Bolognesi
M
M
D000595:Amino Acid Sequence; D000818:Animals; D016948:Azotobacter vinelandii / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D005798:Genes, Bacterial; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*
D001426:Bacterial Proteins; D013884:Thiosulfate Sulfurtransferase