Purification, crystallization and preliminary X-ray crystallographic analysis of 23S RNA m2G2445 methyltransferase RlmL from Escherichia coli
Research output: Contribution to journal › Journal article › Research › peer-review
The RlmL (YcbY) protein in Escherichia coli is an rRNA methyltransferase that is specific for m2G2445 modification of 23S RNA. The rlmL gene was cloned into the expression vector pET28a and expressed in the host E. coli strain BL21 (DE3). Recombinant protein with a six-histidine tag was purified by Ni2+-affinity chromatography followed by gel filtration. Crystals were grown using the hanging-drop vapour-diffusion method and a detergent was used as an additive to improve diffraction quality. The final crystals diffracted to 2.2 Å resolution. The crystals belonged to space group P21, with unit-cell parameters a = 73.6, b = 140.8, c = 102.9 Å, β = 102.3°. The crystal has a most probable solvent content of 62.8% with two molecules in the asymmetric unit.
Original language | English |
---|---|
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 66 |
Issue number | 11 |
Pages (from-to) | 1484-1486 |
Number of pages | 3 |
ISSN | 1744-3091 |
DOIs | |
Publication status | Published - 1 Nov 2010 |
- Echerichia coli, RlmL, rRNA methyltransferases
Research areas
ID: 234874803