7C9B
Crystal structure of dipeptidase-E from Xenopus laevis
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 | 2019-06-07 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.97949 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 83.775, 40.900, 74.221 |
| Unit cell angles | 90.00, 116.20, 90.00 |
Refinement procedure
| Resolution | 34.840 - 1.400 |
| R-factor | 0.1926 |
| Rwork | 0.191 |
| R-free | 0.22240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6a4s |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.342 |
| Data reduction software | XDS (VERSION Mar 15, 2019 BUILT=20190315) |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | PHENIX (1.19) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 41.500 | 41.500 | 1.310 |
| High resolution limit [Å] | 1.280 | 7.030 | 1.280 |
| Rmerge | 0.066 | 0.057 | 0.468 |
| Rmeas | 0.076 | 0.065 | 0.659 |
| Rpim | 0.036 | 0.032 | 0.464 |
| Total number of observations | 185643 | 1558 | 864 |
| Number of reflections | 49297 | 380 | 703 |
| <I/σ(I)> | 10.7 | 23.5 | 0.9 |
| Completeness [%] | 85.6 | 98.7 | 25.1 |
| Redundancy | 3.8 | 4.1 | 1.2 |
| CC(1/2) | 0.996 | 0.993 | 0.750 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 7 | 294 | 50 mM Bis-Tris, 200 mM NaNO3, 10 mM CaCl2, 30% PEG 3350 |
