1BWR
PROBING THE SUBSTRATE SPECIFICITY OF THE INTRACELLULAR BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE
Experimental procedure
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-11 |
Detector | MARRESEARCH |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 81.056, 81.056, 72.622 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 8.000 - 2.400 |
R-factor | 0.202 * |
Rwork | 0.205 |
R-free | 0.26400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PAF ACETYLHYDROLASE |
RMSD bond length | 0.010 |
RMSD bond angle | 0.031 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.380 |
High resolution limit [Å] | 2.400 | 2.300 |
Number of reflections | 10257 | |
<I/σ(I)> | 18.3 | |
Completeness [%] | 92.0 | 87.6 |
Redundancy | 10.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.8 | pH 6.8 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5-9 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 14 (%) | |
3 | 1 | reservoir | Tris-HCl |