1BP5
HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 113 |
Detector technology | IMAGE PLATE |
Collection date | 1996-11-15 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 83.500, 77.300, 107.500 |
Unit cell angles | 90.00, 98.30, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.200 |
R-factor | 0.203 |
Rwork | 0.203 |
R-free | 0.29200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | INDIVIDUAL DOMAINS OF HUMAN TRANSFERRIN N-TERMINAL HALF-MOLECULE (FE FORM) 1A8E |
RMSD bond length | 0.013 |
RMSD bond angle | 1.700 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 37.000 | 2.200 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.046 | 0.271 |
Number of reflections | 73066 | |
<I/σ(I)> | 9.2 | 4 |
Completeness [%] | 79.9 | 61.1 |
Redundancy | 3.2 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 5.3 | 4 * | PROTEIN WAS CRYSTALLIZED FROM 35% MPD. BUFFER WAS 50MM POTASSIUM ACETATE, PH 5.3, WITH 50MM KCL, AND 20MM NA BICARBONATE CRYSTALS GROWN AT 4 DEGREES C USING THE SITTING DROP METHOD. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | 20 (mM) | ||
3 | 1 | drop | 50 (mM) | ||
4 | 1 | reservoir | potassium acetate | 50 (mM) | |
5 | 1 | reservoir | MPD | 35 (%(v/v)) |