4TUA
Crystal structure of ASL-Thr bound to Codon ACC-A on the Ribosome
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-12-01 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 208.977, 448.713, 621.010 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 68.592 - 3.600 |
| R-factor | 0.2095 |
| Rwork | 0.207 |
| R-free | 0.25180 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3I8F 3I8G 3I8H 3I8I |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.007 |
| Data scaling software | XSCALE |
| Refinement software | PHENIX ((phenix.refine: 1.8.3_1479)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 70.000 | 3.500 | |
| High resolution limit [Å] | 3.400 | 50.000 | 3.400 |
| Rmerge | 0.256 | 0.028 | 1.329 |
| Rmeas | 0.293 | 0.033 | 1.524 |
| Total number of observations | 3230953 | ||
| Number of reflections | 778870 | 219 | 65195 |
| <I/σ(I)> | 5.99 | 31.14 | 1.21 |
| Completeness [%] | 98.2 | 69.3 | 99.4 |
| Redundancy | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 4% PEG 20k, 4% PEG550 MME, 0.1M TRIS-ACETATE, 0.2M KSCN, 10mM MgCl |






