5SSZ
Crystal Structure of wild-type human formylglycine generating enzyme bound to Cu(I)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-07-26 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.999760 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 43.513, 62.024, 110.021 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 55.010 - 1.020 |
R-factor | 0.1313 |
Rwork | 0.131 |
R-free | 0.14170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 55.010 | 55.010 | 1.030 |
High resolution limit [Å] | 1.000 | 4.480 | 1.000 |
Rmerge | 0.037 | 0.026 | 0.331 |
Rmeas | 0.040 | 0.028 | 0.438 |
Total number of observations | 842259 | ||
Number of reflections | 143525 | 2013 | 3230 |
<I/σ(I)> | 21.76 | 51.69 | 1.47 |
Completeness [%] | 89.4 | 99.7 | 27.5 |
Redundancy | 5.868 | 6.792 | 1.654 |
CC(1/2) | 0.999 | 0.999 | 0.787 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 9.6 mg/mL protein in 20mM Tris/HCl pH8.0 mixed 1:1 with reservoir 0.1M Tris/HCl pH 8.5, 20-25% PEG4000, 0.2-0.3M CaCl2 |