4BTB
CRYSTAL STRUCTURE OF THE PEPTIDE(PRO)9 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 | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-10-03 |
| Detector | BRUKER PLATINIUM-135 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 76.930, 53.043, 79.928 |
| Unit cell angles | 90.00, 95.84, 90.00 |
Refinement procedure
| Resolution | 30.262 - 1.899 |
| R-factor | 0.1853 |
| Rwork | 0.183 |
| R-free | 0.23500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2yq8 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.982 |
| Data reduction software | SAINT |
| Data scaling software | SADABS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.600 | 1.940 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.070 | 0.470 |
| Number of reflections | 25406 | |
| <I/σ(I)> | 24.9 | 2.46 |
| Completeness [%] | 99.6 | 94 |
| Redundancy | 13.26 | 6.05 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | 20% PEG 6000, 0.1M BICINE 9, 5MM SPERMINE HCL, 5MM (PRO)9 |
