1XJO
STRUCTURE OF AMINOPEPTIDASE
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12B |
Synchrotron site | NSLS |
Beamline | X12B |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1995-03-25 |
Detector | MAR scanner 300 mm plate |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 61.810, 61.810, 146.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.750 |
R-factor | 0.141 * |
Rwork | 0.141 |
RMSD bond length | 0.020 |
RMSD bond angle | 15.700 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | TNT (5E) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 * |
High resolution limit [Å] | 1.750 * |
Rmerge | 0.054 |
Total number of observations | 244396 * |
Number of reflections | 28606 |
Completeness [%] | 97.0 |
Redundancy | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8 * | 16% PEG 4K, 0.1 M SODIUM ACETATE, pH 5.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | sodium acetate | 0.1 (M) | |
3 | 1 | reservoir | PEG4000 | 16 (%(w/v)) | |
4 | 1 | drop | Tris | 10 (mM) | |
5 | 1 | drop | 20 (mM) | ||
6 | 1 | drop | 1 (mM) |