7CR9
Crystal structure of the N-terminal fragment (residue 1-206) of LonA protease from Meiothermus taiwanensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13C1 |
| Synchrotron site | NSRRC |
| Beamline | BL13C1 |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2015-06-08 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.975 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 32.830, 58.296, 198.492 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.411 - 2.095 |
| R-factor | 0.2114 |
| Rwork | 0.209 |
| R-free | 0.24940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3m65 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.160 |
| High resolution limit [Å] | 2.090 | 2.090 |
| Rmerge | 0.106 | 0.937 |
| Number of reflections | 23209 | 2198 |
| <I/σ(I)> | 17.95 | |
| Completeness [%] | 99.7 | 100 |
| Redundancy | 6.5 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7.5 | 295 | 0.1 M Tris-HCl (pH 7.5), 0.2 M Sodium acetate and 30% PEG 4000 |
