4BT9
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 1-238) TYPE I FROM HUMAN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-19 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.0, 1.9 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 72.280, 100.930, 68.450 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.765 - 1.900 |
| R-factor | 0.1762 |
| Rwork | 0.174 |
| R-free | 0.22250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2yq8 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.931 |
| 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] | 40.000 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.090 | 0.580 |
| Number of reflections | 40153 | |
| <I/σ(I)> | 21.9 | 2.4 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 19.5 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 10% PEGMME 5000, 10% DMSO, 6% MPD, 0.1 M MES, PH 6.0, 5MM SPERMINE HCL, 5MM (PRO-PRO-GLY)3 |
