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 (%) |






