7EP9
The structure of carboxypeptidase from Fusobacterium nucleatum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-11-20 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97934 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 192.004, 124.797, 128.898 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.830 - 2.604 |
R-factor | 0.2317 |
Rwork | 0.229 |
R-free | 0.27380 |
Structure solution method | SAD |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX (1.14_3228) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.700 | |
Number of reflections | 95180 | 94966 |
<I/σ(I)> | 10.2 | |
Completeness [%] | 100.0 | |
Redundancy | 12.7 | |
CC(1/2) | 0.840 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 289.15 | 21%PEG_2000 and 0.1 M Tris pH 7.9 |