Related Experiment Video
Updated: Sep 28, 2026
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Crystallization and preliminary X-ray crystallographic analysis of tRNA(m1G37)methyltransferase from Haemophilus
Hyeon-Woo Kim1, Hyung Jun Ahn, Hye-Jin Yoon
1Structural Proteomics Laboratory, School of Chemistry and Molecular Engineering, Seoul National University, Seoul 151-742, South Korea.
Abstract:
The enzyme tRNA(m(1)G37)methyltransferase (TrmD) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) specifically to guanosine at position 37 within a subset of tRNA species in bacteria. The modified guanosine is next to the anticodon and is important for the maintenance of the correct reading frame during translation. TrmD from Haemophilus influenzae with both N- and C-terminal tags was overexpressed in Escherichia coli and crystallized at 297 K using sodium acetate as a precipitant. Native X-ray diffraction data were collected to 1.85 A resolution. The crystals are rhombohedral, belonging to the space group R32, with unit-cell parameters a = b = 98.05, c = 176.79 A, alpha = beta = 90, gamma = 120 degrees. The presence of one monomer of recombinant TrmD in the crystallographic asymmetric unit gives a V(M) of 3.07 A(3) Da(-1) and a solvent content of 59.9%.
More Related Videos
09:31PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
Published on: September 26, 2020
11:17Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021