6XP0
Structure of human PYCR1 complexed with N-formyl L-proline
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-03-16 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9792 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 164.630, 88.513, 115.462 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 67.026 - 1.950 |
R-factor | 0.1873 |
Rwork | 0.187 |
R-free | 0.20910 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 5uau |
Data reduction software | XDS |
Data scaling software | Aimless (0.7.4) |
Phasing software | PHENIX |
Refinement software | PHENIX (1.14) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 82.320 | 82.320 | 1.980 |
High resolution limit [Å] | 1.950 | 10.680 | 1.950 |
Rmerge | 0.080 | 0.039 | 1.304 |
Rmeas | 0.094 | 0.046 | 1.525 |
Rpim | 0.048 | 0.023 | 0.774 |
Total number of observations | 435036 | 2807 | 22723 |
Number of reflections | 120287 | 802 | 6045 |
<I/σ(I)> | 7.2 | 21.3 | 0.8 |
Completeness [%] | 97.8 | 93.9 | 99.7 |
Redundancy | 3.6 | 3.5 | 3.8 |
CC(1/2) | 0.996 | 0.996 | 0.483 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 295 | Crystallization reservoir contained 250 mM Li2SO4, 19% (w/v) PEG 3350, and 0.1 M HEPES at pH 7.5. Crystal was soaked in cryobuffer containing 100 mM N-formyl L-proline and 20% PEG 200. |