4BVL
Structure of 202-208 deletion mutant of PhaZ7 PHB depolymerase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X13 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-11-19 |
Detector | MARRESEARCH SX-165 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 93.239, 138.829, 172.367 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.558 - 2.002 |
R-factor | 0.119 |
Rwork | 0.115 |
R-free | 0.19080 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4brs |
RMSD bond length | 0.013 |
RMSD bond angle | 1.319 |
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] | 19.600 | 2.120 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.110 | 0.330 |
Number of reflections | 74317 | |
<I/σ(I)> | 12.5 | 4.4 |
Completeness [%] | 98.7 | 94.9 |
Redundancy | 5.2 | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | HANGING DROP VAPOUR DIFFUSION. PROTEIN CONCENTRATION 10 MG/ML. 0.1 M NAOAC (PH 5.0), 0.2 M LICL, 15% W/V PEG6000 |