1VHE
Crystal structure of a aminopeptidase/glucanase homolog
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 32-ID |
| Synchrotron site | APS |
| Beamline | 32-ID |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9795, 0.9641 |
| Spacegroup name | F 4 3 2 |
| Unit cell lengths | 223.966, 223.966, 223.966 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.720 - 1.900 |
| Rwork | 0.176 |
| R-free | 0.19300 |
| Structure solution method | Se-Met MAD phasing |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.600 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (4.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.720 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.130 | 0.292 |
| Number of reflections | 38362 | |
| <I/σ(I)> | 34.7 | 13.1 |
| Completeness [%] | 99.9 | 99.3 |
| Redundancy | 41.8 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | HEPES | 10 (mM) | pH7.5 |
| 2 | 1 | drop | 150 (mM) | ||
| 3 | 1 | drop | methionine | 10 (mM) | |
| 4 | 1 | drop | glycerol | 10 (%) | |
| 5 | 1 | drop | dithiothreitol | 5 (mM) | |
| 6 | 1 | drop | protein | 10 (mg/ml) |
