1GYT
E. coli Aminopeptidase A (PepA)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-07-15 |
Detector | MARRESEARCH |
Spacegroup name | P 32 |
Unit cell lengths | 178.000, 178.000, 244.400 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 500.000 * - 2.500 |
R-factor | 0.183 * |
Rwork | 0.165 |
R-free | 0.21000 * |
Structure solution method | MIR |
RMSD bond length | 0.005 * |
RMSD bond angle | 1.230 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.098 * | 0.307 |
Total number of observations | 1198951 * | |
Number of reflections | 298951 | |
<I/σ(I)> | 11.5 | 3.9 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 8 | 20 MM KCL, 50 MM TRIS PH 8.0, 1 MM MG(AC)2 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 8 (mg/ml) | |
2 | 1 | 2 | 200 (mM) | ||
3 | 1 | 2 | Tris | 50 (mM) | pH8.0 |
4 | 1 | 2 | 1 (mM) |