6UE4
ShyA Endopeptidase from Vibrio cholerae (Closed form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-12-08 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97750 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.115, 87.252, 74.973 |
| Unit cell angles | 90.00, 100.37, 90.00 |
Refinement procedure
| Resolution | 49.550 - 2.080 |
| R-factor | 0.1807 |
| Rwork | 0.178 |
| R-free | 0.23340 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gu1 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 2.007 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.120 |
| High resolution limit [Å] | 2.080 | 2.080 |
| Rmerge | 0.119 | |
| Rmeas | 0.129 | |
| Rpim | 0.049 | |
| Number of reflections | 46469 | 2295 |
| <I/σ(I)> | 4.3 | |
| Completeness [%] | 99.4 | 99.3 |
| Redundancy | 6.7 | 6.6 |
| CC(1/2) | 0.948 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 294 | 0.2 M Malonic Acid pH 6.0, 14% PEG 3350 |
