4HWN
Crystal structure of the second Ig-C2 domain of human Fc-receptor like A (FCRLA), Isoform 9 [NYSGRC-005836]
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-10-18 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0750 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 31.198, 35.517, 73.883 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.941 - 2.006 |
| R-factor | 0.1863 |
| Rwork | 0.184 |
| R-free | 0.22870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3rjd |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.049 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 5.430 | 2.000 |
| Rmerge | 0.070 | 0.059 | 0.213 |
| Number of reflections | 5840 | ||
| <I/σ(I)> | 31.1 | ||
| Completeness [%] | 99.0 | 98 | 100 |
| Redundancy | 10.6 | 9.4 | 11.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | Protein (20 mM Hepes, pH 7.5, 150 mM NaCl, 10% glycerol; Reservoir (0.1M Sodium Cacodylate pH 6.5, 0.2M Sodium Chloride, 2M Ammonium Sulfate); Cryoprotection (Reservoir + 2M Lithium Sulfate), Sitting Drop Vapor Diffusion, temperature 298K, VAPOR DIFFUSION, SITTING DROP |






