4BT8
CRYSTAL STRUCTURE OF THE APO FORM OF N-TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE TYPE I FROM HUMAN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-10 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 71.939, 105.403, 65.991 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.630 - 2.198 |
| R-factor | 0.2204 |
| Rwork | 0.218 |
| R-free | 0.26140 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2yq8 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.182 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.600 | 2.330 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.050 | 0.530 |
| Number of reflections | 25805 | |
| <I/σ(I)> | 15.9 | 2.3 |
| Completeness [%] | 98.4 | 97.6 |
| Redundancy | 4 | 3.85 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 25-30% PEG400, 10% ISOPROPANOL, 100MM HEPES PH 7.5, 5MM SPERMINE HCL |
