6VIN
Crystallographic structure of the circularly permuted human Taspase1 protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-08-05 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 1.0332 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 196.000, 196.000, 196.910 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.050 - 3.040 |
| R-factor | 0.2435 |
| Rwork | 0.237 |
| R-free | 0.30740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6ugk |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.744 |
| Data reduction software | XDS |
| Data scaling software | STARANISO |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.050 | 3.110 |
| High resolution limit [Å] | 3.040 | 3.040 |
| Rmerge | 0.068 | 1.800 |
| Number of reflections | 15315 | 15315 |
| <I/σ(I)> | 21.2 | |
| Completeness [%] | 93.9 | |
| Redundancy | 19.6 | |
| CC(1/2) | 1.000 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4 | 293 | 0.1 M sodium citrate pH 4.0, 1.0 M ammonium sulfate, 10% 2-methyl-2,4-pentanediol (MPD), and 0.4 M NaCl |
