5W25
Crystal structure of Aspartyl-tRNA synthetase from Mycobacterium tuberculosis complexed with L-Aspartic Acid
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-05-03 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 64.720, 158.240, 75.740 |
Unit cell angles | 90.00, 93.77, 90.00 |
Refinement procedure
Resolution | 43.254 - 2.650 |
R-factor | 0.2257 |
Rwork | 0.225 |
R-free | 0.24500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4rmf |
RMSD bond length | 0.002 |
RMSD bond angle | 0.460 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MoRDa |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 43.254 | 43.254 | 2.720 |
High resolution limit [Å] | 2.650 | 11.850 | 2.650 |
Rmerge | 0.049 | 0.021 | 0.517 |
Rmeas | 0.056 | 0.024 | 0.592 |
Total number of observations | 182369 | ||
Number of reflections | 44023 | 505 | 3273 |
<I/σ(I)> | 16.48 | 43.23 | 2.59 |
Completeness [%] | 99.8 | 97.5 | 99.7 |
Redundancy | 4.143 | 3.871 | 4.253 |
CC(1/2) | 0.999 | 0.999 | 0.948 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 290 | MytuD.00145.b.M1.PD00305 at 10.3 mg/ml was incubated with 1 mM L-aspartic acid, then mixed 1:1 with Morpheus (h1): 10% (w/v) PEG-20000, 20% (v/v) PEG MME 550, 0.1 M MES/imidazole, pH = 6.5, 0.02 M each L-glutamate, DL-alanine, glycine, DL-lysine, DL-serine, Tray 251523h1, puck gdy9-5 |