1IWD
Proposed Amino Acid Sequence and the 1.63 Angstrom X-ray Crystal Structure of a Plant Cysteine Protease Ervatamin B: Insight into the Structural Basis of its Stability and Substrate Specificity.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-03-09 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.200, 58.760, 69.350 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 * - 1.630 |
| R-factor | 0.161 |
| Rwork | 0.161 |
| R-free | 0.18400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2act |
| RMSD bond length | 0.005 |
| RMSD bond angle | 23.800 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.670 |
| High resolution limit [Å] | 1.630 | 1.630 |
| Rmerge | 0.048 | 0.281 |
| Total number of observations | 142404 * | |
| Number of reflections | 25294 * | |
| <I/σ(I)> | 24.06 | 4 |
| Completeness [%] | 99.1 | 89.2 |
| Redundancy | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 292 | PEG4000, Tris HCl, Magnesium Chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12.9 (mg/ml) | |
| 2 | 1 | reservoir | Tris-HCl | 5 (mM) | |
| 3 | 1 | reservoir | 0.1 (M) | ||
| 4 | 1 | reservoir | PEG4000 | 15 (%) | pH8.5 |
