1EH3
R210K 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 RAXIS IIC |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 124.440, 57.180, 57.340 |
| Unit cell angles | 90.00, 117.09, 90.00 |
Refinement procedure
| Resolution | 6.000 - 2.000 |
| Rwork | 0.198 |
| R-free | 0.25000 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 23.900 * |
| 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] | 2.070 | |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.073 | 0.265 |
| Number of reflections | 23444 | |
| <I/σ(I)> | 9.9 | |
| Completeness [%] | 95.8 | 97.1 |
| Redundancy | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 8 | 277 | HEPES, NaCl, pH 8.0, LIQUID DIFFUSION, temperature 4K |
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) |
