1ILD
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 4.6
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 1999-01-15 |
Detector | MAC Science DIP-2000 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 78.484, 78.484, 101.669 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.800 |
R-factor | 0.211 * |
Rwork | 0.211 |
R-free | 0.27500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1QD5 MUTATED ACTIVE SITE RESIDUES to ALA AND GAVE ALL ATOMS A RANDOM SHIFT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.850 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.064 | 0.343 |
Total number of observations | 98747 * | |
Number of reflections | 9276 | 453 * |
<I/σ(I)> | 25.4 | 4.9 |
Completeness [%] | 99.3 | 99.6 |
Redundancy | 10 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.6 * | 293 | MPD, calcium chloride, Bis-Tris buffer, pH 6.0, 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) |