1OQG
Crystal structure of the D63E mutant of the N-lobe human transferrin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 113 |
| Detector technology | AREA DETECTOR |
| Collection date | 2002-05-08 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.307, 57.312, 135.383 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.245 |
| Rwork | 0.245 |
| R-free | 0.26100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1a8e |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.300 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.050 | 0.137 |
| Number of reflections | 26077 | |
| <I/σ(I)> | 20.1 | 10.2 |
| Completeness [%] | 92.5 | 91.1 * |
| Redundancy | 3.6 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 18 * | used microseeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 35 (mg/ml) | |
| 2 | 1 | drop | ammonium bicarbonate | 0.1 (M) | pH7.4 |
| 3 | 1 | reservoir | potassium acetate | 0.2 (M) | pH7.4 |
| 4 | 1 | reservoir | PEG3350 | 16-22 (%) |
