7LX8
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) | 0.9537 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.289, 60.289, 96.328 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 45.903 - 1.030 |
| R-factor | 0.2066 |
| Rwork | 0.206 |
| R-free | 0.21220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4w57 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.756 |
| 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] | 48.160 | 48.160 | 1.050 |
| High resolution limit [Å] | 1.030 | 5.640 | 1.030 |
| Rmerge | 0.048 | 0.028 | 2.634 |
| Rmeas | 0.049 | 0.028 | 2.817 |
| Rpim | 0.011 | 0.006 | 0.974 |
| Total number of observations | 1733212 | 13315 | 33145 |
| Number of reflections | 99343 | 721 | 4185 |
| <I/σ(I)> | 21.5 | 74.7 | 0.7 |
| Completeness [%] | 98.8 | 99.9 | 86.7 |
| Redundancy | 17.4 | 18.5 | 7.9 |
| CC(1/2) | 1.000 | 1.000 | 0.355 |
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 |
