7L3I
T4 Lysozyme L99A - propylbenzene - RT
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 278 |
| Detector technology | PIXEL |
| Collection date | 2018-03-15 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.977, 60.977, 97.268 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.774 - 1.460 |
| R-factor | 0.1493 |
| Rwork | 0.148 |
| R-free | 0.16800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4w51 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.692 |
| Data reduction software | xia2 |
| Data scaling software | xia2 |
| Phasing software | PHASER (2.8.2) |
| Refinement software | PHENIX (1.14-3260) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 48.630 | 48.630 | 1.500 |
| High resolution limit [Å] | 1.460 | 6.530 | 1.460 |
| Rmerge | 0.065 | 0.040 | 0.865 |
| Number of reflections | 37038 | 2028 | 1836 |
| <I/σ(I)> | 13.5 | ||
| Completeness [%] | 100.0 | 99.8 | 100 |
| Redundancy | 6.6 | 6 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | Crystals were grown from a 10 mg/mL frozen protein solution by the hanging drop method at 291-293K, with a 1:1 drop ratio of protein to solution and over a well solution of 0.1 M Tris-hydrochloride (pH 8), 20%-26% (w/v) PEG 4000, 70-170 mM lithium citrate, 8%-18% 2-propanol, 50 mM 2-mercaptoethanol, and 50 mM 2-hydroxyethyl disulfide |
