2Y22
Human AlphaB-crystallin Domain (residues 67-157)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-06-25 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 67.280, 78.340, 131.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 59.890 - 3.700 |
R-factor | 0.2162 |
Rwork | 0.213 |
R-free | 0.27700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2y1y |
RMSD bond length | 0.008 |
RMSD bond angle | 1.070 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | BUSTER (2.8.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 67.400 | 3.900 |
High resolution limit [Å] | 3.700 | 3.700 |
Rmerge | 0.240 | 0.660 |
Number of reflections | 7861 | |
<I/σ(I)> | 8.7 | 4 |
Completeness [%] | 100.0 | 100 |
Redundancy | 12.8 | 13.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | SITTING DROPS WITH 20 MG/ML PROTEIN IN 25 MM TRIS, PH 8.5, 200 MM NACL EQUILIBRATED AGAINST 110 MM BICINE, PH 9.0, 55% MPD |