5KIN
Crystal structure of tryptophan synthase alpha beta complex from Streptococcus pneumoniae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-02-16 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9793373 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.697, 71.160, 138.682 |
| Unit cell angles | 90.00, 101.69, 90.00 |
Refinement procedure
| Resolution | 49.126 - 2.450 |
| R-factor | 0.1828 |
| Rwork | 0.180 |
| R-free | 0.22750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4neg |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.508 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | PHENIX (dev_2386) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.490 |
| High resolution limit [Å] | 2.450 | 6.650 | 2.450 |
| Rmerge | 0.141 | 0.057 | 0.740 |
| Rmeas | 0.166 | 0.068 | 0.880 |
| Rpim | 0.088 | 0.037 | 0.472 |
| Total number of observations | 174816 | ||
| Number of reflections | 48447 | ||
| <I/σ(I)> | 7.4 | ||
| Completeness [%] | 99.7 | 97.8 | 99.8 |
| Redundancy | 3.6 | 3.3 | 3.3 |
| CC(1/2) | 0.991 | 0.683 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 297 | 0.2 M Ammonium Acetate, 0.1 M Tris-Cl, 25% PEG3350 |
