7BJT
Structure-function analysis of a new PL17 oligoalginate lyase from the marine bacterium Zobellia galactanivorans DsijT
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 | 2016-12-03 |
| Detector | DECTRIS PILATUS3 100K-M |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 65 |
| Unit cell lengths | 163.390, 163.390, 166.730 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 43.700 - 1.420 |
| R-factor | 0.1616 |
| Rwork | 0.161 |
| R-free | 0.17040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ojz |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.231 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.700 | 1.470 |
| High resolution limit [Å] | 1.420 | 1.420 |
| Rmerge | 0.840 | |
| Rpim | 0.183 | |
| Number of reflections | 444259 | 32662 |
| <I/σ(I)> | 4.74 | |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 5.66 | 5 |
| CC(1/2) | 0.998 | 0.656 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 292 | protein solution of 11.3 mg.ml-1 concentration. Drops of 2 micro-l volume of this protein solution were mixed with 1 micro-l of crystallization solution that contained 2.1 M DL-Malic acid pH 7.0, and equilibrated against a reservoir containing 500 micro-l. |
