1C8C
CRYSTAL STRUCTURES OF THE CHROMOSOMAL PROTEINS SSO7D/SAC7D BOUND TO DNA CONTAINING T-G MISMATCHED BASE PAIRS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 123 |
Detector technology | IMAGE PLATE |
Collection date | 1998-08-15 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.475, 49.800, 37.681 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.450 |
R-factor | 0.229 |
R-free | 0.28680 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1azp |
RMSD bond length | 0.009 * |
RMSD bond angle | 2.300 * |
Phasing software | AMoRE |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 1.380 | 1.450 * |
Rmerge | 0.054 | |
Number of reflections | 14498 | |
Completeness [%] | 89.1 | 63 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.5 | PROTEIN WAS CRYSTALLIZED FROM 1.3MM SSO7D, 1.3MM DUPLEX DNA, 2.5 MM TRIS (PH 6.5), 2.5% PEG 400, EQUILIBRATED AGAINST 15% PEG 400 at pH 6.5, VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents
ID | crystal ID | solution ID | reagent name | concentration | details |
1 | 1 | 1 | TRIS | ||
2 | 1 | 1 | PEG 400 | ||
3 | 1 | 2 | PEG 400 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Sso7d | 1.3 (mM) | |
2 | 1 | drop | DNA duplex | 1.3 (mM) | |
3 | 1 | drop | Tris-HCl | 2.5 (mM) | |
4 | 1 | drop | PEG400 | 2.5 (%) | |
5 | 1 | reservoir | PEG400 | 15 (%) |