1OQH
Crystal Structure of the R124A 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 | 2002-05-12 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 43.930, 57.120, 135.250 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.400 |
R-factor | 0.219 |
Rwork | 0.219 |
R-free | 0.28800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1a8e |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.510 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.100 | 0.430 |
Number of reflections | 12875 * | |
<I/σ(I)> | 7.4 | 2.2 |
Completeness [%] | 91.5 | 91.4 |
Redundancy | 3.3 | 2.9 * |
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 (%) |