1TAL
ALPHA-LYTIC PROTEASE AT 120 K (SINGLE STRUCTURE MODEL)
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 1992-07-25 |
| Detector | MARRESEARCH |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 65.800, 65.800, 79.500 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 1.500 |
| R-factor | 0.165 |
| Rwork | 0.165 |
| R-free | 0.19200 |
| Structure solution method | REFINEMENT OF 2ALP |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.310 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.570 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.059 | |
| Total number of observations | 148867 * | |
| Number of reflections | 31458 * | |
| Completeness [%] | 99.0 | 99.1 |
| Redundancy | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | pH 8.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | reservoir | 1.3 (M) | ||
| 3 | 1 | reservoir | Tris-HCl | 20 (mM) |






