1QRC
TAILSPIKE PROTEIN, MUTANT W391A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 287 |
| Detector technology | AREA DETECTOR |
| Collection date | 1998-08-02 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 120.900, 120.900, 120.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.500 |
| R-factor | 0.149 |
| Rwork | 0.149 |
| RMSD bond length | 0.010 * |
| RMSD bond angle | 1.670 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((AGROVATA) |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.630 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.132 | 0.330 |
| Total number of observations | 54352 * | |
| Number of reflections | 19727 | |
| <I/σ(I)> | 8 | |
| Completeness [%] | 96.2 * | 97.2 |
| Redundancy | 2.8 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 10 | 4 * | Steinbacher, S., (1994) Science, 265, 383. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium sulfate | 1.0 (M) | |
| 2 | 1 | reservoir | sodium phosphate | 0.1 (M) | |
| 3 | 1 | drop | protein | 10 (mg/ml) | |
| 4 | 1 | drop | HEPES | 10 (mM) | |
| 5 | 1 | drop | ammonium sulfate | 1.5 (M) | |
| 6 | 1 | drop | sodium phosphate | 0.1 (M) |
