2V5F
Crystal structure of wild type peptide-binding domain of human type I collagen prolyl 4-hydroxylase.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR591 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-04-10 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 37.472, 59.046, 61.668 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.650 - 2.030 |
| R-factor | 0.199 |
| Rwork | 0.196 |
| R-free | 0.26500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tjc |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.497 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.4.0077) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.600 | 2.140 |
| High resolution limit [Å] | 2.030 | 2.030 |
| Rmerge | 0.050 | 0.160 |
| Number of reflections | 9304 | |
| <I/σ(I)> | 21 | 10.1 |
| Completeness [%] | 98.8 | 93.2 |
| Redundancy | 5.6 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9.5 | PROTEIN WAS CRYSTALLIZED FROM 1 M NA CITRATE, 100 MM CHES, PH 9.5. |
