8BD0
Human Gamma-D crystallin R36S mutant with DTT-Cystein Protein modification
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2) |
Synchrotron site | PETRA III, EMBL c/o DESY |
Beamline | P14 (MX2) |
Temperature [K] | 298 |
Detector technology | PIXEL |
Collection date | 2019-12-01 |
Detector | DECTRIS EIGER X 1M |
Wavelength(s) | 0.98 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 53.900, 83.700, 101.000 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 101.000 - 2.000 |
R-factor | 0.20727 |
Rwork | 0.204 |
R-free | 0.24971 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2g98 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.492 |
Data reduction software | CrystFEL |
Data scaling software | CrystFEL |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 101.130 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 31629 | 3090 |
<I/σ(I)> | 2.71 | 0.6 |
Completeness [%] | 100.0 | 100 |
Redundancy | 50.3 | 34.7 |
CC(1/2) | 0.996 | 0.140 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | BATCH MODE | 7.8 | 298 | 50 mM phosphate buffer pH 7.8, 20 mM DTT |