4EKP
T4 Lysozyme L99A/M102H with Nitrobenzene 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 | 48.370, 75.530, 52.720 |
| Unit cell angles | 90.00, 93.22, 90.00 |
Refinement procedure
| Resolution | 43.185 - 1.640 |
| R-factor | 0.1705 |
| Rwork | 0.169 |
| R-free | 0.19630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4e97 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.057 |
| 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 | 1.730 |
| High resolution limit [Å] | 1.640 | 10.000 | 1.640 |
| Rmerge | 0.046 | 0.013 | 0.335 |
| Number of reflections | 45872 | 202 | 6794 |
| <I/σ(I)> | 15.9 | 52.79 | 3 |
| Completeness [%] | 98.8 | 91.8 | 99.1 |
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 |
