7L38
T4 Lysozyme L99A - Apo - cryo
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-07-15 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 59.835, 59.835, 96.334 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 51.819 - 1.330 |
R-factor | 0.1793 |
Rwork | 0.178 |
R-free | 0.19950 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4w51 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.715 |
Data reduction software | xia2 |
Data scaling software | xia2 |
Phasing software | PHASER (2.8.0) |
Refinement software | PHENIX (1.14-3260) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 51.820 | 1.350 |
High resolution limit [Å] | 1.330 | 1.330 |
Rmerge | 0.070 | |
Number of reflections | 46473 | 2270 |
<I/σ(I)> | 9.1 | |
Completeness [%] | 99.9 | |
Redundancy | 6 | |
CC(1/2) | 0.995 | 0.867 |
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 |