4V2I
Biochemical characterization and structural analysis of a new cold- active and salt tolerant esterase from the marine bacterium Thalassospira sp
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-02-08 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 73.326, 85.429, 91.747 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.866 - 1.686 |
| R-factor | 0.1451 |
| Rwork | 0.143 |
| R-free | 0.18210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qz3 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.177 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.790 |
| High resolution limit [Å] | 1.690 | 1.690 |
| Rmerge | 0.100 | 0.620 |
| Number of reflections | 61330 | |
| <I/σ(I)> | 13.6 | 2.4 |
| Completeness [%] | 93.4 | 63.3 |
| Redundancy | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | THE PROTEIN WAS AT 10 MG/ML IN 50 MM TRIS-HCL PH 8.0, 500 MM NACL AND 10% GLYCEROL. RESERVOIR: 25% PEG 3350, 0.2 M MGCL2 |
