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 |