1I6B
STRUCTURE OF EQUINE APOLACTOFERRIN AT 3.2 A RESOLUTION USING CRYSTALS GROWN AT 303K
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 288 |
Detector technology | IMAGE PLATE |
Collection date | 2000-02-16 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 80.490, 103.480, 112.270 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.200 |
R-factor | 0.222 |
Rwork | 0.222 |
R-free | 0.29100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MARE DIFFERIC LACTOFERRIN COORDINATES |
RMSD bond length | 0.014 |
RMSD bond angle | 1.700 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 20.000 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmerge | 0.110 * | 0.380 * |
Total number of observations | 67331 * | |
Number of reflections | 15800 * | |
<I/σ(I)> | 7 | 11 |
Completeness [%] | 99.4 * | 94.7 * |
Redundancy | 3.2 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICRODIALYSIS | 8 | 303 | ethanol, pH 8.0, MICRODIALYSIS, temperature 303K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 70 (mg/ml) | |
2 | 1 | 1 | Tris-HCl | 0.025 (M) | pH8.0 |
3 | 1 | 2 | ethanol | 19 (%(v/v)) |