1H44
R210L N-TERMINAL LOBE HUMAN LACTOFERRIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 113 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU IMAGE PLATE |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 125.108, 57.065, 57.559 |
| Unit cell angles | 90.00, 117.19, 90.00 |
Refinement procedure
| Resolution | 32.000 * - 2.000 |
| R-factor | 0.203 |
| Rwork | 0.203 |
| R-free | 0.24000 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lct |
| RMSD bond length | 0.005 * |
| RMSD bond angle | 23.400 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.077 | 0.294 |
| Number of reflections | 23271 | |
| <I/σ(I)> | 11.9 | 3.5 |
| Completeness [%] | 94.4 | 89 |
| Redundancy | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 8 | 4 * | HEPES, NACL, pH 8.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 28 (mg/ml) | |
| 2 | 1 | 1 | HEPES | 20 (mM) | |
| 3 | 1 | 1 | 1 (M) | pH8.0 |
