1AOV
APO DUCK OVOTRANSFERRIN
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX7.2 |
Synchrotron site | SRS |
Beamline | PX7.2 |
Temperature [K] | 277 |
Detector technology | FILM |
Collection date | 1989-05 |
Detector | FILM |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 77.620, 98.740, 126.960 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 4.000 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.32000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dot |
RMSD bond length | 0.016 |
RMSD bond angle | 25.400 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | X-PLOR (3.0) |
Refinement software | X-PLOR (3.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 4.200 |
High resolution limit [Å] | 4.000 | 4.000 |
Rmerge | 0.090 | 0.110 |
Number of reflections | 7487 | |
<I/σ(I)> | 10.2 | 3 |
Completeness [%] | 92.8 | 50 |
Redundancy | 4.1 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 * | PROTEIN WAS CRYSTALLIZED FROM 15 - 30% PEG 6000, PH 6., pH 6.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | sodium acetate | 0.01 (M) | |
2 | 1 | reservoir | PEG6000 | 15-30 (%) | |
3 | 1 | drop | protein | 30 (mg/ml) | |
4 | 1 | drop | sodium acetate | 0.01 (M) | |
5 | 1 | drop | PEG6000 | 17 (%) |