1SXR
Drosophila Peptidoglycan Recognition Protein (PGRP)-SA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-09-13 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.069 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 136.290, 64.420, 45.870 |
| Unit cell angles | 90.00, 100.33, 90.00 |
Refinement procedure
| Resolution | 45.000 - 1.560 |
| R-factor | 0.181 |
| Rwork | 0.177 |
| R-free | 0.21100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1oht |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.299 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.9999) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.130 | 1.620 |
| High resolution limit [Å] | 1.560 | 1.560 |
| Rmerge | 0.056 | 0.451 |
| Number of reflections | 54845 | |
| <I/σ(I)> | 10.7 | 2 |
| Completeness [%] | 99.4 | 94 |
| Redundancy | 3.6 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 295 | 1.3 to 1.5 M Li2SO4 and 0.1 M MES , pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
