1E21
Ribonuclease 1 des1-7 Crystal Structure at 1.9A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-02-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 32.691, 42.733, 79.894 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| R-factor | 0.1959 |
| Rwork | 0.196 |
| R-free | 0.25110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7rsa |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.610 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.135 | 0.364 * |
| Total number of observations | 27390 * | |
| Number of reflections | 8618 | |
| <I/σ(I)> | 4.4 | 2 |
| Completeness [%] | 92.9 | 87.2 |
| Redundancy | 3.2 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.5 | 7% PEG 8K, 0.1M TRIS-HCL PH 8.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | reservoir | PEG8000 | 7 (%(v/v)) | |
| 3 | 1 | reservoir | Tris-HCl | 0.1 (M) |
