1TJC
Crystal structure of peptide-substrate-binding domain of human type I collagen prolyl 4-hydroxylase
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-01-01 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9814, 0.9811, 0.9745 |
Spacegroup name | P 32 |
Unit cell lengths | 55.980, 55.980, 105.430 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 35.580 - 2.300 |
R-factor | 0.2257 |
Rwork | 0.224 |
R-free | 0.25872 |
Structure solution method | MAD |
RMSD bond length | 0.018 |
RMSD bond angle | 1.677 |
Data scaling software | XDS |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.400 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.038 | 0.258 |
Number of reflections | 16195 | |
<I/σ(I)> | 15.66 | 3.7 |
Completeness [%] | 98.7 | 99.2 |
Redundancy | 3.16 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.4 | 277 | ammonium phosphate, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K |