N-terminal domain of Plasmodium berghei glutamyl-tRNA synthetase (native crystal structure)

2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.

1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.

Solution X-ray scattering highlights discrepancies in Plasmodium multi-aminoacyl-tRNA synthetase complexes.

Discovery of two distinct aminoacyl-tRNA synthetase complexes anchored to the Plasmodium surface tRNA import protein.

A2, B2, C2, D2, E2: insertion (cloning artifact)

Small and fragile crystals initially diffracting only at 5 angstroms were obtained. Their diffraction limit was further improved up to 2.7 angstroms by microseeding.

Protein concentration: 6 to 9 mg/mL
0.1 M HEPS-NaOH pH 7.5, 1.4-1.5 M ammonium sulfate, 20% (v/v) glycerol and using microseeding.

N-terminal GST-like domain of Plasmodium berghei cytosolic glutamyl-tRNA synthetase

N-terminal GST-like domain of Plasmodium berghei tRNA import protein

The scaffold of Plasmodium berghei multi aminoacyl-tRNA synthetase complexes

Plasmodium berghei multi aminoacyl-tRNA synthetase complex, Q-complex containing the GST-like domains of tRNA import protein, glutamyl-tRNA synthetase and glutaminyl-tRNA synthetase

Plasmodium berghei multi aminoacyl-tRNA synthetase complex, M-complex containing the GST-like domains of tRNA import protein, glutamyl-tRNA synthetase and methionyl-tRNA synthetase

aminoacyl-tRNA synthetase, tRNA, RNA binding protein, protein complex, Cell surface protein, multi-aminoacyl-tRNA synthetase complex (MARS-MSC), GST-like domain, aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMP)