1V0S
Uninhibited form of Phospholipase D from Streptomyces sp. strain PMF
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 57.410, 57.370, 68.620 |
Unit cell angles | 90.00, 93.45, 90.00 |
Refinement procedure
Resolution | 69.010 - 1.750 |
R-factor | 0.153 |
Rwork | 0.151 |
R-free | 0.20600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | BASED ON PDB ENTRY 1F0I |
RMSD bond length | 0.019 |
RMSD bond angle | 1.761 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 69.010 | |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.080 | |
Number of reflections | 39534 | |
<I/σ(I)> | 8.4 | |
Completeness [%] | 92.1 | |
Redundancy | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.4 | 0.2 M NH4AC, 0.1 M CITRATE/ PHOSPHATE BUFFER AT PH5.4, 27.5% PEG 4000. CRYSTALS WERE THEREAFTER BACKSOAKED TWICE IN A PHOSPHATE-FREE BUFFER TO REMOVE TRACE-AMOUNTS OF PHOSPHATE IN THE ACTIVE SITE., pH 5.40 |