3RY3
Putative solute-binding protein from Yersinia pestis.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-07-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 157.036, 171.322, 128.842 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.100 - 2.430 |
| R-factor | 0.1745 |
| Rwork | 0.173 |
| R-free | 0.20800 |
| Structure solution method | SAD |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.634 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 43.100 | 50.000 | 2.510 |
| High resolution limit [Å] | 2.430 | 6.700 | 2.430 |
| Rmerge | 0.121 | 0.065 | 0.804 |
| Number of reflections | 64629 | ||
| <I/σ(I)> | 8.3 | 2.32 | |
| Completeness [%] | 100.0 | 99.9 | 99.9 |
| Redundancy | 7.3 | 6.9 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 2.8 M sodium acetate trihydrate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
