4KDW
Crystal structure of a bacterial immunoglobulin-like domain from the M. primoryensis ice-binding adhesin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 93 |
| Detector technology | CCD |
| Collection date | 2012-12-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Spacegroup name | P 1 |
| Unit cell lengths | 25.640, 28.620, 32.250 |
| Unit cell angles | 97.02, 112.93, 96.88 |
Refinement procedure
| Resolution | 29.190 - 1.350 |
| R-factor | 0.132 |
| Rwork | 0.130 |
| R-free | 0.16500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4kdv |
| RMSD bond length | 0.025 |
| RMSD bond angle | 2.244 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.191 | 1.420 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.049 | 0.085 |
| Number of reflections | 17224 | |
| <I/σ(I)> | 10.33 | 10.7 |
| Completeness [%] | 95.1 | 91.6 |
| Redundancy | 3.6 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 8.5 | 298 | 20% PEG 4000, 0.2M CaCl2, 0.1M Tris-HCl, microbatch, pH 8.5, EVAPORATION, temperature 298.0K |
