1E7N
The N-terminal domain of beta-B2-crystallin resembles the putative ancestral homodimer
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY |
Synchrotron site | Photon Factory |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 65 |
Unit cell lengths | 110.960, 110.960, 29.880 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.890 - 2.350 |
R-factor | 0.212 |
Rwork | 0.212 |
R-free | 0.24600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 * |
RMSD bond angle | 1.260 * |
Phasing software | CNS (0.9) |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 2.350 |
Rmerge | 0.050 * |
Number of reflections | 9079 |
Completeness [%] | 99.8 |
Redundancy | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 4 * | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6 (mg/ml) | |
2 | 1 | reservoir | magnesium acetate tetrahydrate | 0.2 (M) | |
3 | 1 | reservoir | sodium cacodylate | 0.1 (M) | |
4 | 1 | reservoir | PEG8000 | 15 (%(w/v)) |