4EKQ
T4 Lysozyme L99A/M102H with 4-Nitrophenol Bound
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 | CCD |
| Collection date | 2010-11-22 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.116 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 48.210, 76.070, 52.810 |
| Unit cell angles | 90.00, 93.01, 90.00 |
Refinement procedure
| Resolution | 48.143 - 1.540 |
| R-factor | 0.1763 |
| Rwork | 0.175 |
| R-free | 0.20410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4e97 |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.775 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHENIX (1.7.1_743) |
| Refinement software | PHENIX (1.7.1_743) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.620 |
| High resolution limit [Å] | 1.540 | 4.870 | 1.540 |
| Rmerge | 0.043 | 0.020 | 0.337 |
| Number of reflections | 52590 | 1536 | 7600 |
| <I/σ(I)> | 15.77 | 46.09 | 3.11 |
| Completeness [%] | 93.4 | 84.1 | 96.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 277 | 30% (w/v) PEG-6000, 0.3 M LiSO4, 3% (w/v) TMAO, 50 mM 2-mercaptoethanol, 50 mM 2-hydroxyethyl disulfide, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
