1PWT
THERMODYNAMIC ANALYSIS OF ALPHA-SPECTRIN SH3 AND TWO OF ITS CIRCULAR PERMUTANTS WITH DIFFERENT LOOP LENGTHS: DISCERNING THE REASONS FOR RAPID FOLDING IN PROTEINS
Experimental procedure
| Source details | OTHER |
| Temperature [K] | 287 |
| Detector technology | IMAGE PLATE |
| Detector | MAR scanner 180 mm plate |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 33.000, 42.400, 49.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 14.500 - 1.770 |
| R-factor | 0.189 |
| Rwork | 0.187 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1shg |
| RMSD bond length | 0.011 |
| RMSD bond angle | 0.029 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.800 |
| High resolution limit [Å] | 1.770 | 1.770 |
| Rmerge | 0.050 | 0.200 |
| Total number of observations | 43628 * | |
| Number of reflections | 7163 | |
| <I/σ(I)> | 25.1 | 5.9 |
| Completeness [%] | 99.8 | 96.8 |
| Redundancy | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4 | pH 4 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 6 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 1.1 (M) | |
| 3 | 1 | reservoir | sodium citrate/citric acid | 90 (mM) | |
| 4 | 1 | reservoir | Bis-Tris propane | 90 (mM) | |
| 5 | 1 | reservoir | EDTA | 0.9 (mM) | |
| 6 | 1 | reservoir | dithiothreitol | 0.9 (mM) | |
| 7 | 1 | reservoir | sodium azide | 0.9 (mM) |
