1SNQ
PROTEIN STABILITY IN STAPHYLOCOCCAL NUCLEASE
Experimental procedure
| Temperature [K] | 277 |
| Detector technology | IMAGE PLATE |
| Collection date | 1993-02 |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | P 41 |
| Unit cell lengths | 49.180, 49.180, 63.510 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 1.950 * |
| R-factor | 0.187 |
| Rwork | 0.187 |
| R-free | 0.27400 |
| RMSD bond length | 0.011 * |
| RMSD bond angle | 1.602 * |
| Data reduction software | R-AXIS |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 9999.000 * | |
| High resolution limit [Å] | 1.950 * | 1.950 * |
| Rmerge | 0.047 | |
| Total number of observations | 30773 * | |
| Number of reflections | 10604 | |
| Completeness [%] | 94.5 | 90 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8.15 | 4 * | Loll, P.J., (1989) Proteins: Struct.,Funct., Genet., 5, 183. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | drop | 20 (mg/ml) | |
| 2 | 1 | drop | potassium phosphate | 10.5 (mM) | |
| 3 | 1 | drop | MPD | 17 (%(w/w)) | |
| 4 | 1 | drop | 10 (mM) | ||
| 5 | 1 | drop | potassium citrate | 20 (mM) | |
| 6 | 1 | reservoir | potassium phosphate | 10.5 (mM) | |
| 7 | 1 | reservoir | MPD | 20-30 (%(w/w)) |






