3LIP
OPEN CONFORMATION OF PSEUDOMONAS CEPACIA LIPASE
Experimental procedure
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Temperature [K] | 283 |
Detector technology | IMAGE PLATE |
Collection date | 1994-05 |
Detector | MARRESEARCH |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 91.300, 47.300, 85.400 |
Unit cell angles | 90.00, 121.40, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.000 |
Rwork | 0.188 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1cvl |
RMSD bond length | 0.020 |
RMSD bond angle | 0.039 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | PROLSQ |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.700 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.095 * | |
Total number of observations | 33550 * | |
Number of reflections | 17688 | |
Completeness [%] | 83.3 | 83.1 |
Redundancy | 2 | 1.63 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.5 * | 12 * | 29-30 % N-PROPANOL, 0.1 M TRIS HCL BUFFER, PH 8.4-8.7, AT 12 DEGREES IN FOUR WEEKS, PROTEIN CONCENTRATION 22 MG/ML, temperature 285K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | 1-propanol | 29-30 (%(v/v)) | |
2 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.5-8.7 |
3 | 1 | drop | protein | 22 (mg/ml) | |
4 | 1 | drop | Tris-HCl | 10 (mM) | pH7.5 |