1VPF
STRUCTURE OF HUMAN VASCULAR ENDOTHELIAL GROWTH FACTOR
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-12 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.190, 59.810, 77.520 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.500 |
R-factor | 0.205 |
Rwork | 0.205 |
R-free | 0.29700 |
Structure solution method | MIR |
RMSD bond length | 0.013 |
RMSD bond angle | 26.800 * |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | X-PLOR (3.8) |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.041 * | |
Number of reflections | 17684 | |
<I/σ(I)> | 56.5 | |
Completeness [%] | 97.0 | 96 |
Redundancy | 3.6 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.5 * | Christinger, H.W., (1996) Proteins: Struct.,Funct., Genet., 26, 353. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10-15 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | drop | 0.4 (M) | ||
4 | 1 | reservoir | PEG3350 | 14 (%) | |
5 | 1 | reservoir | isopropanol | 20 (%) | |
6 | 1 | reservoir | ammonium acetate | 0.2 (M) | |
7 | 1 | reservoir | 0.2 (M) | ||
8 | 1 | reservoir | 0.4 (M) |