8J9D
Crystal structure of M61 peptidase (bestatin-bound) from Xanthomonas campestris
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | RRCAT INDUS-2 BEAMLINE PX-BL21 |
| Synchrotron site | RRCAT INDUS-2 |
| Beamline | PX-BL21 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-03-02 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.979490 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 105.008, 95.196, 144.489 |
| Unit cell angles | 90.00, 104.47, 90.00 |
Refinement procedure
| Resolution | 44.360 - 1.900 |
| R-factor | 0.1722 |
| Rwork | 0.171 |
| R-free | 0.19090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.727 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.600 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.066 | 0.395 |
| Rmeas | 0.080 | 0.495 |
| Rpim | 0.045 | 0.293 |
| Number of reflections | 215479 | 9862 |
| <I/σ(I)> | 13.4 | 2.3 |
| Completeness [%] | 99.4 | 92.4 |
| Redundancy | 2.9 | |
| CC(1/2) | 0.997 | 0.828 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 8.5 | 294 | 0.1M Tris-Cl pH 8.5, 0.1M NaCl, 6-11% (w/v) PEG 4000 |
