PMID:12554950
| Citation |
Choe, HW, Jeong, DG, Park, JH, Schlesinger, R, Labahn, J, Hofmann, KP and Büldt, G (2003) Preliminary X-ray characterization of the ribonuclease P (C5 protein) from Escherichia coli: expression, crystallization and cryoconditions. Acta Crystallogr. D Biol. Crystallogr. 59:350-2 |
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| Abstract |
The gene for Escherichia coli ribonuclease P (RNase P) protein (also known as C5 protein) and its mutant C5-C113A have been expressed as GST fusion proteins in E. coli at a high level. After cleavage of the fusion protein, highly purified functional C5 protein is obtained that can be crystallized with 2.5-2.6 M (NH(4))(2)HPO(4)/(NH(4))H(2)PO(4) pH 7.0 at room temperature. These crystals are suitable for X-ray analysis, belong to the space group P3(1)21 or P3(2)21 (unit-cell parameters a = b = 66.67, c = 142.09 A) and diffract to 2.9 A at 100 K using sorbitol and glycerol as cryoprotectants. For three molecules in the asymmetric unit a V(M) of 2.17 A(3) Da(-1) was calculated. |
| Links | |
| Keywords |
Amino Acid Substitution; Cryoprotective Agents/chemistry; Crystallization; Crystallography, X-Ray; Endoribonucleases/chemistry; Endoribonucleases/genetics; Endoribonucleases/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Glutathione Transferase/genetics; Glycerol/chemistry; RNA, Catalytic/chemistry; RNA, Catalytic/genetics; RNA, Catalytic/metabolism; Recombinant Fusion Proteins/biosynthesis; Recombinant Fusion Proteins/genetics; Ribonuclease P; Ribonucleoproteins/chemistry; Ribonucleoproteins/genetics; Ribonucleoproteins/metabolism; Sorbitol/chemistry |
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