1FR5
PHAGE FR CAPSIDS WITH A FOUR RESIDUE DELETION IN THE COAT PROTEIN FG LOOP
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-01-21 |
| Detector | MARRESEARCH |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 264.100, 264.100, 654.200 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 3.500 |
| R-factor | 0.256 |
| Rwork | 0.256 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1frs |
| RMSD bond length | 0.016 |
| RMSD bond angle | 26.200 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.560 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmerge | 0.139 | 0.387 |
| Number of reflections | 52800 | 1419 * |
| <I/σ(I)> | 6.9 | |
| Completeness [%] | 48.0 | 26 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 20 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | ammonium sulfate | 10 (%sat) | |
| 2 | 1 | drop | Mops | 50 (mM) | |
| 3 | 1 | drop | 0.02 (%(w/v)) | ||
| 4 | 1 | reservoir | ammonium sulfate | 30 (%sat) | |
| 5 | 1 | reservoir | Mops | 50 (mM) |
