4J3G
Crystal structure of Ribosomal-protein-alanine N-acetyltransferase from Brucella melitensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-09-19 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 0.9774 |
| Spacegroup name | P 1 |
| Unit cell lengths | 39.110, 57.000, 73.420 |
| Unit cell angles | 86.55, 88.15, 88.76 |
Refinement procedure
| Resolution | 46.320 - 1.750 |
| R-factor | 0.1727 |
| Rwork | 0.171 |
| R-free | 0.21190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2j8m |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.323 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (2.5.1) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.800 |
| High resolution limit [Å] | 1.750 | 7.830 | 1.750 |
| Rmerge | 0.058 | 0.027 | 0.457 |
| Number of reflections | 62171 | 706 | 4563 |
| <I/σ(I)> | 16.27 | 46.02 | 2.81 |
| Completeness [%] | 97.4 | 99.2 | 96 |
| Redundancy | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 290 | Microlytics MCSG1, 200mM ammoinum sulfate, 100mM HEPES/NaOH pH 7.5, 25% PEG 3350, BrabA.17352.a.A1.PS01094 at 20mg/ml, VAPOR DIFFUSION, SITTING DROP, temperature 290K |
