7L37
T4 Lysozyme L99A - Apo - 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 | 2018-03-18 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 61.006, 61.006, 98.529 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 36.031 - 1.439 |
R-factor | 0.1565 |
Rwork | 0.155 |
R-free | 0.18450 |
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 |
Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.260 | 1.460 |
High resolution limit [Å] | 1.439 | 1.439 |
Rmerge | 0.061 | 0.852 |
Number of reflections | 39149 | 1868 |
<I/σ(I)> | 15.5 | |
Completeness [%] | 99.9 | 96.8 |
Redundancy | 9.9 | 9 |
CC(1/2) | 0.999 | 0.545 |
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 |