1BIY
STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 288 |
Detector technology | IMAGE PLATE |
Collection date | 1996-05 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.797, 101.436, 76.275 |
Unit cell angles | 90.00, 104.88, 90.00 |
Refinement procedure
Resolution | 17.000 - 3.370 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.29600 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HUMAN DIFERRIC LACTOFERRIN |
RMSD bond length | 0.010 |
RMSD bond angle | 27.200 * |
Data reduction software | MARSCALE |
Data scaling software | MARSCALE |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 17.000 | 3.580 |
High resolution limit [Å] | 3.300 * | 3.300 * |
Rmerge | 0.051 | 0.093 * |
Total number of observations | 42104 * | |
Number of reflections | 11711 | |
<I/σ(I)> | 34.47 | 13.35 |
Completeness [%] | 98.5 * | 60 * |
Redundancy | 3.68 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | 8 | 277 * | pH 8.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 50 (mg/ml) | |
2 | 1 | 1 | Tris-HCl | 0.025 (M) | |
3 | 1 | 2 | ethanol | 19 (%(v/v)) | |
4 | 1 | 2 | Tris-HCl | 0.025 (M) |