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 (%) |