1H2L
Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX14.2 |
Synchrotron site | SRS |
Beamline | PX14.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-05-15 |
Detector | ADSC CCD |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 86.264, 86.264, 147.914 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.000 - 2.250 |
R-factor | 0.185 |
Rwork | 0.183 |
R-free | 0.21700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.404 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.630 | 2.370 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.058 | 0.307 |
Number of reflections | 27294 | |
<I/σ(I)> | 9.7 | 2.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7 | 7.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 17 * | 1.2M AMMONIUM SULPHATE, 4% PEG400, 0.1M HEPES PH7.5, ARGON ATMOSPHERE, 11MG/ML PROTEIN WITH 1MM FE(II), 2.5MM AKG AND 2.5MM PEPTIDE, pH 7.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 1.2 (M) | |
2 | 1 | reservoir | PEG400 | 4 (%) | |
3 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |
4 | 1 | drop | FIH | 11 (mg/ml) | |
5 | 1 | drop | Fe2+ | 1 (mM) | |
6 | 1 | drop | 2OG/NOG | 2 (mM) | |
7 | 1 | drop | CAD fragment | 1 (mM) |