7OBM
Crystal structure of the human Prolyl Endopeptidase-Like protein short form (residues 90-727)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-12 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.979420 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 64.920, 150.880, 220.660 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.670 - 3.100 |
R-factor | 0.2469 |
Rwork | 0.245 |
R-free | 0.28210 |
Structure solution method | SAD |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.19_4092) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.670 | 48.670 | 3.180 |
High resolution limit [Å] | 3.100 | 13.860 | 3.100 |
Rmerge | 0.094 | 0.026 | 1.295 |
Rmeas | 0.109 | 0.030 | 1.504 |
Total number of observations | 149099 | ||
Number of reflections | 37971 | 416 | 2797 |
<I/σ(I)> | 11.53 | 42.79 | 0.99 |
Completeness [%] | 99.9 | 96.5 | 99.9 |
Redundancy | 3.927 | 3.714 | 3.921 |
CC(1/2) | 0.998 | 0.999 | 0.428 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 200 nL of protein and 200 nL of reservoir were combined in a MRC SD2 crystallization plate by a Mosquito crystallization robot. The reservoir solution consisted of 2M ammonium sulfate and 0.1 M NaHEPES buffer, pH 7.5. The protein solution was 9.1mg/ml Nd88 PREPL, 5 mM HEPES, pH 7.5, 50 mM NaCL, 0.3 mM TCEP. Crystals were observed after one year incubation in the cold room. |