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 |