3U8E
Crystal Structure of Cysteine Protease from Bulbs of Crocus sativus at 1.3 A Resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Detector technology | CCD |
| Wavelength(s) | 0.97740 |
| Spacegroup name | H 3 |
| Unit cell lengths | 97.970, 97.970, 48.780 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 24.490 - 1.310 |
| R-factor | 0.1893 |
| Rwork | 0.144 |
| R-free | 0.18930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2b1m |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP (in CCP4i) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | |
| High resolution limit [Å] | 1.310 | 1.310 |
| Number of reflections | 41920 | |
| Completeness [%] | 99.9 | 97.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 0.085M tri-Sodium citrate, 0.85M Lithium sulphate, 0.425M Ammonium sulfate, 15% (v/v) Glycerol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
