7L3B
T4 Lysozyme L99A - iodobenzene - 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 | 60.750, 60.750, 97.921 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 35.841 - 1.270 |
R-factor | 0.1498 |
Rwork | 0.149 |
R-free | 0.16720 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4w51 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.741 |
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] | 46.350 | 46.350 | 1.300 |
High resolution limit [Å] | 1.270 | 5.680 | 1.270 |
Rmerge | 0.072 | 0.060 | 1.347 |
Number of reflections | 55886 | 3011 | 2753 |
<I/σ(I)> | 14.1 | ||
Completeness [%] | 100.0 | 98.9 | 100 |
Redundancy | 8.2 | 7.2 | 8.3 |
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 |