2.7.1.148	-	672138	
2.7.1.148	Hi-trap chelating columns are used for the purification of recombinant 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase	699633	
2.7.1.148	recombinant enzyme	349728, 722218	
2.7.1.148	recombinant GST-tagged enzyme from Escherichia coli strain DH5alpha by glutathione affinity chromatography, tag cleavage through Prescission protease, followed by anion exchange chromatography, and gel filtration	747328	
2.7.1.148	recombinant His-tagged enzyme from strain BL21(DE3) to homogeneity by nickel affinity and anion exchange chromatography	663207	
2.7.1.148	recombinant His6-tagged enzyme by nickel affinity chromatography	660700	
2.7.1.148	recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage through thrombin, followed by anion exchange chromatography, and gel filtration	747328	
2.7.1.148	recombinant selenomethionine-labeled enzyme from Escherichia coli strain B834(DE3) by ammonium sulfate fractionation, hydrophobic interaction and heparin affinity chromatography, gel filtration, and ultrafiltration	662149	
2.7.1.148	The gene is preceded by a His6 tag to enable purification of the recombinant protein via metal-chelating affinity chromatography. The polyhistidine tag is removed by thrombin-mediated proteolysis, followed by purification with anion-exchange chromatography. Purity of the sample is assessed by SDS-PAGE and MALDI-TOF MS.	686699