7YWP
Closed conformation of Oligopeptidase B from Serratia proteomaculans with covalently bound TCK
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-05-31 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9677 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 75.529, 89.660, 108.650 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.310 - 2.200 |
R-factor | 0.1879 |
Rwork | 0.184 |
R-free | 0.25440 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7ob1 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.566 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.078 | 0.190 |
Rmeas | 0.090 | 0.270 |
Number of reflections | 37524 | 5487 |
<I/σ(I)> | 6.6952 | 3.89 |
Completeness [%] | 98.6 | 99.9 |
Redundancy | 4.14 | 4.27 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 277 | 200 mM Lithium sulfate, 100 mM Bis-Tris pH 5.5, 23% PEG 3350 |