1HWG
1:2 COMPLEX OF HUMAN GROWTH HORMONE WITH ITS SOLUBLE BINDING PROTEIN
Experimental procedure
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1994-10 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 145.610, 69.020, 76.040 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.199 |
Rwork | 0.199 |
R-free | 0.28700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2HHR |
RMSD bond length | 0.009 |
RMSD bond angle | 1.530 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 * | 2.700 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.097 * | 0.313 * |
Number of reflections | 25222 | |
<I/σ(I)> | 9 | 2.7 |
Completeness [%] | 94.3 | 81.2 |
Redundancy | 4.6 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.25 * | 18 * | THE PROTEIN COMPLEX WAS CRYSTALLISED AT PH 6.5 USING 45% (W/V) LISO4 WITH 2% PEG-500 DME AND SOAKED TO PH 5.5 PRIOR TO DATA COLLECTION |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | 46 (%(v/v)sat) | ||
2 | 1 | reservoir | PEG500 | 2 (%) | |
3 | 1 | drop | protein | 10 (mg/ml) |