5E3I
Crystal Structure of a Histidyl-tRNA synthetase from Acinetobacter baumannii with bound L-Histidine and ATP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-04-21 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 88.810, 103.070, 246.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.540 - 2.200 |
R-factor | 0.1661 |
Rwork | 0.165 |
R-free | 0.20540 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1kmm |
RMSD bond length | 0.007 |
RMSD bond angle | 0.910 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | BALBES |
Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.260 |
High resolution limit [Å] | 2.200 | 9.840 | 2.200 |
Rmerge | 0.077 | 0.029 | 0.533 |
Rmeas | 0.084 | 0.032 | 0.580 |
Total number of observations | 352039 | ||
Number of reflections | 57675 | 696 | 4195 |
<I/σ(I)> | 15.55 | 32.7 | 3.79 |
Completeness [%] | 99.9 | 94.6 | 100 |
Redundancy | 6.1 | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 290 | AcbaC.00063.a.B1.PW37682 at 19.5 mg/ml incubated with 3 mM L-Histidine, ATP, and MgCl2, then then mixed 1:1 with MCSG1(e3): 50mM MgCl2, 0.1M Hepes, pH=7.5, 30% PEG-MME550, cryoprotected with 20% ethylene glycol |