1LQB
Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-11-30 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 58.940, 58.940, 243.380 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 * - 2.000 |
| R-factor | 0.225 |
| Rwork | 0.225 |
| R-free | 0.27800 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1VCB.pdb |
| RMSD bond length | 0.006 |
| RMSD bond angle | 23.800 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.060 * | 0.490 * |
| Total number of observations | 448657 * | |
| Number of reflections | 24245 | |
| <I/σ(I)> | 20 | 1 |
| Completeness [%] | 76.0 | 30 |
| Redundancy | 18.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 22 * | HEPES, PEG2000 monomethylester, ammonium sulfate, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 2 | 1 | reservoir | HEPES | 100 (mM) | pH7.4 |
| 3 | 1 | reservoir | PEG2000MME | 40 (%) | |
| 4 | 1 | reservoir | ammonium sulfate | 200 (mM) |
