PMID:10739928
| Citation |
Grimm, C, Klebe, G, Ficner, R and Reuter, K (2000) Screening orthologs as an important variable in crystallization: preliminary X-ray diffraction studies of the tRNA-modifying enzyme S-adenosyl-methionine:tRNA ribosyl transferase/isomerase. Acta Crystallogr. D Biol. Crystallogr. 56:484-8 |
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| Abstract |
The genes encoding the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyl transferase/isomerase (QueA) from 12 eubacterial sources were overexpressed in Escherichia coli and the resulting products were purified to homogeneity and subjected to crystallization trials. Using the hanging-drop vapour-diffusion method, crystals suitable for X-ray diffraction experiments were only obtained for the queA gene product from Bacillus subtilis. The crystals belong to the space group P422, with unit-cell parameters a = b = 100.7, c = 150.9 A. Using highly focused synchrotron radiation from the EMBL/ESRF beamline ID13 (Grenoble, France), diffraction to at least 3.2 A could be achieved. A selenomethionyl derivative of the protein was prepared and crystallized for future multiwavelength anomalous diffraction (MAD) experiments. |
| Links | |
| Keywords |
Bacteria/enzymology; Bacteria/genetics; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Isomerases; Pentosyltransferases/chemistry; Pentosyltransferases/isolation & purification; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification |
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