4BTA
CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N- TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-244) TYPE I FROM HUMAN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X12 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-12-14 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 234.660, 47.850, 60.290 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.800 - 2.950 |
| R-factor | 0.2296 |
| Rwork | 0.227 |
| R-free | 0.27940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2yq8 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.798 |
| 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] | 33.600 | 3.030 |
| High resolution limit [Å] | 2.950 | 2.950 |
| Rmerge | 0.080 | 0.760 |
| Number of reflections | 14997 | |
| <I/σ(I)> | 15.01 | 2.33 |
| Completeness [%] | 99.5 | 99.1 |
| Redundancy | 5.01 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 10% PEGMME5000, 10% DMSO, 10% MPD, 0.1 M MES, PH 6.0, 5MM (PRO-PRO-GLY)3 |
