3RS1
Mouse C-type lectin-related protein Clrg
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-05-12 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.91841 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 118.310, 61.380, 32.360 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.390 - 1.940 |
| R-factor | 0.18641 |
| Rwork | 0.185 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hup |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.336 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.080 | 0.306 |
| Number of reflections | 17372 | |
| <I/σ(I)> | 10.4 | 4.5 |
| Completeness [%] | 96.0 | 90 |
| Redundancy | 5.6 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | spontaneous crystallization | 7.5 | 293 | spontaneous crystallization on tube wall; buffer: 10 mM HEPES, pH 7.5, 100 mM NaCl and 1 mM NaN3, 2.3 mg/ml, temperature 293K |
