1FOU
CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-08-14 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 177.160, 169.240, 185.440 |
| Unit cell angles | 90.00, 114.10, 90.00 |
Refinement procedure
| Resolution | 9.000 - 3.200 |
| R-factor | 0.27 |
| Rwork | 0.290 |
| R-free | 0.36000 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.600 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 9.000 | 3.240 |
| High resolution limit [Å] | 3.200 * | 3.210 |
| Rmerge | 0.065 * | 0.198 |
| Number of reflections | 78035 | |
| <I/σ(I)> | 21 | |
| Completeness [%] | 99.5 | 100 |
| Redundancy | 3.9 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.5 * | 292 | Badasso, M.O., (2000) Acta Crystallogr. D56, 1187. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 7-10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 5 (mM) | |
| 3 | 1 | drop | 0.4 (M) | ||
| 4 | 1 | drop | HEPES | 0.1 (M) | |
| 5 | 1 | drop | 0.2 (M) | ||
| 6 | 1 | reservoir | MPD | 0.2 (M) | |
| 7 | 1 | reservoir | HEPES | 0.1 (M) |
