1G02
Ribonuclease T1 V16S mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-01-27 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.398, 50.061, 47.035 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 1.940 - 1.870 * |
| R-factor | 0.182 |
| Rwork | 0.179 |
| R-free | 0.21100 * |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.408 |
| 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] | 20.000 | 1.940 |
| High resolution limit [Å] | 1.860 | 1.860 |
| Rmerge | 0.160 | 0.603 |
| Total number of observations | 73803 * | |
| Number of reflections | 7969 * | |
| <I/σ(I)> | 11.7 | |
| Completeness [%] | 94.9 | 90.8 |
| Redundancy | 9.3 | 9.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.2 * | 298 | Zegers, I., (1998) Nat.Struct.Biol., 5, 280. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mM) | |
| 2 | 1 | drop | 2'GMP | 2 (mM) | |
| 3 | 1 | drop | 20 (mM) | ||
| 4 | 1 | drop | 2 (mM) | ||
| 5 | 1 | reservoir | MPD | 55 (%(v/v)) |
