7LX7
T4 lysozyme mutant L99A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-11-24 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.95386 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.255, 60.255, 96.212 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 52.182 - 1.050 |
| R-factor | 0.1941 |
| Rwork | 0.194 |
| R-free | 0.20210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4w57 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.785 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 96.210 | 96.210 | 1.070 |
| High resolution limit [Å] | 1.050 | 5.750 | 1.050 |
| Rmerge | 0.052 | 0.024 | 2.143 |
| Rmeas | 0.054 | 0.025 | 2.242 |
| Rpim | 0.012 | 0.006 | 0.639 |
| Total number of observations | 1712996 | 12792 | 42246 |
| Number of reflections | 92402 | 684 | 3652 |
| <I/σ(I)> | 22.9 | 92.3 | 1.2 |
| Completeness [%] | 97.6 | 99.9 | 79.2 |
| Redundancy | 18.5 | 18.7 | 11.6 |
| CC(1/2) | 1.000 | 0.999 | 0.404 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 294 | Isopropanol, PEG 4000, Tris-Cl pH 8.0, Beta-mercaptoethanol, 2-hyrdoxyethyl disulfide |
