4XPK
The crystal structure of Campylobacter jejuni N-acetyltransferase PseH
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 | CCD |
| Collection date | 2014-10-29 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9796 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 42.558, 111.033, 41.045 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.950 |
| R-factor | 0.1989 |
| Rwork | 0.197 |
| R-free | 0.23290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4jjx |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.555 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 4.200 | 1.950 |
| Rmerge | 0.066 | 0.041 | 0.421 |
| Rmeas | 0.073 | 0.045 | 0.464 |
| Rpim | 0.031 | 0.019 | 0.191 |
| Total number of observations | 79770 | ||
| Number of reflections | 14574 | ||
| <I/σ(I)> | 23.2 | ||
| Completeness [%] | 98.3 | 97.6 | 99.5 |
| Redundancy | 5.5 | 5.1 | 5.6 |
| CC(1/2) | 0.999 | 0.904 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 291 | 22-24% PEG MME 550, 4mM reduced glutathione, 4mM oxidized glutathione, 0.1M phosphate-citrate |
