1HDF
Evolution of the eye lens beta-gamma-crystallin domain fold
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Wavelength(s) | 0.95, 0.97885, 0.9791 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 41.350, 41.350, 213.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.350 |
R-factor | 0.239 |
Rwork | 0.239 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.162 |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 2.350 |
Rmerge | 0.057 |
Number of reflections | 10284 |
<I/σ(I)> | 26.4 |
Completeness [%] | 99.5 |
Redundancy | 5.56 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.6 | pH 4.60 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 30 (mg/ml) | |
2 | 1 | reservoir | calcium chloride | 0.2 (M) | |
3 | 1 | reservoir | sodium acetate | 0.2 (M) | |
4 | 1 | reservoir | 2-propanol | 20 (%(w/v)) |