5ISV
Crystal structure of the ribosomal-protein-S18-alanine N-acetyltransferase from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-02-08 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97857 |
| Spacegroup name | P 1 |
| Unit cell lengths | 40.222, 41.785, 46.404 |
| Unit cell angles | 93.74, 90.08, 116.52 |
Refinement procedure
| Resolution | 30.000 - 1.350 |
| R-factor | 0.15837 |
| Rwork | 0.156 |
| R-free | 0.20902 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2cnt |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.662 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.370 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.045 | 0.335 |
| Number of reflections | 56272 | |
| <I/σ(I)> | 38.05 | 3.3 |
| Completeness [%] | 95.0 | 90 |
| Redundancy | 3.9 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.01 M tri-sodium citrate, 33% (w/v) PEG6000 |
