1GGP
CRYSTAL STRUCTURE OF TRICHOSANTHES KIRILOWII LECTIN-1 AND ITS RELATION TO THE TYPE 2 RIBOSOME INACTIVATING PROTEINS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.960, 69.870, 180.960 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.700 |
| R-factor | 0.225 |
| Rwork | 0.225 |
| R-free | 0.30000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1abr |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| 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] | 30.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Number of reflections | 12480 | |
| <I/σ(I)> | 7.4 | 2 |
| Completeness [%] | 74.0 | 68 |
| Redundancy | 2.9 | 2.95 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | Using the hanging-drop method, in which the droplets consisted of equal volume protein solution (4.2mg/ml) and the reservoir solution containing 15% PEG 8000, 0.5M Li2SO4 and 0.1M sodium cacodylate buffer (pH 6.5). , pH 6.0 |
