1A8E
HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1990-05 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.120, 57.910, 135.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.600 |
R-factor | 0.181 * |
Rwork | 0.181 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | RABBIT TRANSFERRIN |
RMSD bond length | 0.014 |
RMSD bond angle | 20.700 * |
Data reduction software | R-AXIS (SOFTWARE) |
Data scaling software | R-AXIS |
Refinement software | TNT (5E) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 1.600 |
Rmerge | 0.061 |
Number of reflections | 39418 |
<I/σ(I)> | 14.6 |
Completeness [%] | 82.4 |
Redundancy | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.75 | 4 * | PROTEIN WAS CRYSTALLIZED FROM 26% PEG 4000. BUFFER WAS 40MM NA CACODYLATE, PH 5.75, WITH 20MM NA BICARBONATE. CRYSTALS GROWN AT 4 DEGREES C USING THE HANGING DROP METHOD., vapor diffusion - hanging drop, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | sodium cacodylate | 40 (mM) | |
2 | 1 | reservoir | sodium bicarbonate | 20 (mM) | |
3 | 1 | reservoir | PEG4000 | 26 (%) |