1CJR
X-RAY CRYSTALLOGRAPHIC STUDIES OF DENATURATION IN RIBONUCLEASE S
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 44.650, 44.650, 98.100 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.300 |
R-factor | 0.234 * |
Rwork | 0.245 |
R-free | 0.27000 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 24.700 * |
Data reduction software | AUTOMAR |
Data scaling software | XDS |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 2.400 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.070 | |
Number of reflections | 4968 | |
Completeness [%] | 86.0 | 86 |
Redundancy | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 5.5 * | Kim, E.E., (1992) Biochemistry, 31, 12304. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12.5 (mg/ml) | |
2 | 1 | drop | 6.0 (M) | ||
3 | 1 | drop | sodium acetate | 0.1 (M) | |
4 | 1 | reservoir | 80 (%sat) | ||
5 | 1 | reservoir | sodium acetate | 0.1 (M) |