1ILZ
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 6.1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Wavelength(s) | 1.00 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 78.168, 78.168, 101.685 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 31.000 - 2.500 |
R-factor | 0.222 * |
Rwork | 0.222 |
R-free | 0.26800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Starting model 1QD5 with the active site residues truncated to ala and all waters and detergent molecules removed. All remaining atoms have been given a random shift of almost 0.5 Angstrom in all directions. |
RMSD bond length | 0.006 |
RMSD bond angle | 1.136 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.000 | 2.540 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.037 | 0.113 |
Total number of observations | 150605 * | |
Number of reflections | 12728 * | 611 * |
<I/σ(I)> | 39.2 | 8.3 |
Completeness [%] | 98.8 | 96.1 |
Redundancy | 11.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.6 * | 293 | MPD, calcium chloride, bis-tris buffer, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | MPD | 27 (%(v/v)) | |
2 | 1 | reservoir | 0.4-1.0 (mM) | ||
3 | 1 | reservoir | Bis-Tris | 0.1 (M) | |
4 | 1 | drop | protein | 10 (mg/ml) | |
5 | 1 | drop | 10 (mM) | ||
6 | 1 | drop | OGP | 1 (%(w/v)) | |
7 | 1 | drop | Tris-HCl | 0.2 (mM) |