1AY2
STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 290 |
| Detector technology | IMAGE PLATE |
| Collection date | 1993-05 |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 2 |
| Unit cell lengths | 127.580, 121.080, 26.860 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.600 |
| R-factor | 0.194 |
| Rwork | 0.194 |
| Structure solution method | MIR |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.359 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((AGROVATA) |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.000 | 2.780 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.081 * | |
| Number of reflections | 6494 | |
| <I/σ(I)> | 6.7 | 2.3 |
| Completeness [%] | 95.0 | 80.2 |
| Redundancy | 4 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | Parge, H.E., (1990) J. Biol. Chem., 265, 2278. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 1 (%(w/v)) | |
| 10 | 1 | reservoir | 0.02 (%) | ||
| 2 | 1 | drop | BOG | 1-1.5 (%) | |
| 3 | 1 | drop | Tris-HCl | 100 (mM) | |
| 4 | 1 | drop | 20 (mM) | ||
| 5 | 1 | drop | dithiothreitol | 1 (mM) | |
| 6 | 1 | drop | 0.02 (%) | ||
| 7 | 1 | drop | PEG400 | 36-45 (%) | |
| 8 | 1 | reservoir | Tris-HCl | 100 (mM) | |
| 9 | 1 | drop | reservoir |
