5XYK
Structure of Transferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 5C (4A) |
| Synchrotron site | PAL/PLS |
| Beamline | 5C (4A) |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-11-15 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 50.059, 50.059, 201.242 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 67.080 - 2.570 |
| R-factor | 0.26242 |
| Rwork | 0.261 |
| R-free | 0.28586 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5h5y |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.653 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 67.080 |
| High resolution limit [Å] | 2.570 |
| Number of reflections | 9052 |
| <I/σ(I)> | 3.4 |
| Completeness [%] | 94.9 |
| Redundancy | 7.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION, RECRYSTALLIZATION | 5.5 | 290 | 0.2M ammonium acetate 0.1M Bis-Tris pH5.5 25% PEG2250 |
