1JQF
Human Transferrin N-Lobe Mutant H249Q
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 110 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-10-01 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.200, 57.200, 135.750 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.850 |
| R-factor | 0.221 * |
| Rwork | 0.221 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1a8e |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.250 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.087 | 0.394 |
| Number of reflections | 30081 * | |
| <I/σ(I)> | 17 | 2.9 |
| Completeness [%] | 99.4 | 96.5 |
| Redundancy | 4.6 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 291 | used microseeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 35 (mg/ml) | |
| 2 | 1 | reservoir | potassium acetate | 0.1 (M) | |
| 3 | 1 | reservoir | PEG3350 | 20-25 (%) |






