2FCK
Structure of a putative ribosomal-protein-serine acetyltransferase from Vibrio cholerae.
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 105 |
| Detector technology | CCD |
| Collection date | 2005-03-29 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97915, 0.97929 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 53.051, 103.065, 37.861 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.700 |
| R-factor | 0.21239 |
| Rwork | 0.211 |
| R-free | 0.24394 |
| Structure solution method | MAD |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.681 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.744 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Number of reflections | 22626 | |
| Completeness [%] | 95.8 | 86.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.1M Bis-Tris propane, 4M NaNO3, sucrose, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
