5EQT
crystal structure of the ATPase domain of PAN from Pyrococcus horikoshii
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-10-31 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 114.344, 46.488, 56.428 |
| Unit cell angles | 90.00, 115.18, 90.00 |
Refinement procedure
| Resolution | 47.948 - 1.943 |
| R-factor | 0.2237 |
| Rwork | 0.223 |
| R-free | 0.23920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3h4m chain A |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.621 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.21) |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.946 | 47.946 | 2.050 |
| High resolution limit [Å] | 1.943 | 6.150 | 1.940 |
| Rmerge | 0.046 | 1.248 | |
| Rmeas | 0.081 | ||
| Rpim | 0.031 | 0.020 | 0.576 |
| Total number of observations | 132669 | 4315 | 17090 |
| Number of reflections | 19463 | ||
| <I/σ(I)> | 9.7 | 28.9 | 1.1 |
| Completeness [%] | 97.7 | 99.8 | 93.1 |
| Redundancy | 6.8 | 6.4 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | NaCH3COO 0.1 M pH 5.5, NH4PO4 0.6 M |
