1I2F
Ribonuclease T1 V16A mutant, form II
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-01-20 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.393, 42.773, 56.664 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.950 |
| R-factor | 0.172 * |
| Rwork | 0.172 |
| R-free | 0.20460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 25.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.138 | 0.431 |
| Total number of observations | 29804 * | |
| Number of reflections | 7382 | |
| <I/σ(I)> | 8.4 | 3.44 |
| Completeness [%] | 97.6 | 86.7 |
| Redundancy | 4.04 | 3.81 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.2 | 293 | Zegers, I., (1998) Nat.Struct.Biol., 5, 280. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | RNase T1 | 15 (mg/ml) | |
| 2 | 1 | drop | exo-cGPS | 15 (mM) | |
| 3 | 1 | drop | 20 (mM) | ||
| 4 | 1 | drop | 2 (mM) | ||
| 5 | 1 | reservoir | MPD | 55 (%(v/v)) |
