3TCV
Crystal structure of a GCN5-related N-acetyltransferase from Brucella melitensis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-06-16 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 1.03322 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 102.490, 66.860, 91.690 |
Unit cell angles | 90.00, 107.51, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.750 |
R-factor | 0.1626 |
Rwork | 0.161 |
R-free | 0.18950 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3pzj |
RMSD bond length | 0.011 |
RMSD bond angle | 1.388 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER (2.3.0) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.800 | |
High resolution limit [Å] | 1.750 | 7.830 | 1.750 |
Rmerge | 0.067 | 0.022 | 0.453 |
Number of reflections | 58008 | 650 | 3617 |
<I/σ(I)> | 13.81 | 37.61 | 2.65 |
Completeness [%] | 97.1 | 91.2 | 82.3 |
Redundancy | 3.7 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | BrabA.17403.a.A1 OS01078 at 28.7 mg/mL against JCSG+ condition A3 0.2 M ammonium citrate, 20% PEG 3350 with 25% ethylene glycol as cryo-protectant, crystal tracking ID 223197a3, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |