1AL0
PROCAPSID OF BACTERIOPHAGE PHIX174
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 277 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-01 |
| Detector | FUJI |
| Spacegroup name | I 21 3 |
| Unit cell lengths | 774.000, 774.000, 774.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 3.500 |
| R-factor | 0.316 |
| Rwork | 0.316 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1PHX |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 45.000 |
| High resolution limit [Å] | 3.500 |
| Rmerge | 0.247 |
| Total number of observations | 1646040 * |
| Number of reflections | 527445 |
| Completeness [%] | 55.3 |
| Redundancy | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | PROCAPSIDS WERE CRYSTALLIZED BY VAPOUR DIFFUSION FROM 43-37% (OF SATURATION) AMMONIUM SULFATE, 100MM MES PH6.0, vapor diffusion |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15-20 (mg/ml) | |
| 2 | 1 | drop | Tris | 10 (mM) | |
| 3 | 1 | drop | 0.25 (M) | ||
| 4 | 1 | drop | EDTA | 5 (mM) | |
| 5 | 1 | drop | 5 (mM) | ||
| 6 | 1 | reservoir | ammonium sulfate | 42-47 (%sat) | |
| 7 | 1 | reservoir | MES | 0.1 (M) |
