4XWY
Crystal structure of human sepiapterin reductase in complex with an N-acetylserotinin analogue
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-12-11 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.99999 |
Spacegroup name | P 61 |
Unit cell lengths | 144.840, 144.840, 180.695 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 125.435 - 2.350 |
R-factor | 0.1868 |
Rwork | 0.185 |
R-free | 0.21670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4hwk |
RMSD bond length | 0.008 |
RMSD bond angle | 1.219 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.21) |
Phasing software | MOLREP (11.2.08) |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 125.435 | 46.308 | 2.480 |
High resolution limit [Å] | 2.350 | 7.430 | 2.350 |
Rmerge | 0.035 | 0.716 | |
Rmeas | 0.100 | ||
Rpim | 0.030 | 0.011 | 0.220 |
Total number of observations | 998773 | 31832 | 149858 |
Number of reflections | 89220 | ||
<I/σ(I)> | 15.8 | 44.9 | 3.4 |
Completeness [%] | 100.0 | 99.6 | 100 |
Redundancy | 11.2 | 11.1 | 11.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 2% W/V PEG1000, 2.5% V/V glycerol, 1.7 M Ammonium sulfate, 0.1 M Hepes |