3M1B
Crystal structure of human FcRn with a dimeric peptide inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Collection date | 2009-02-01 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.050, 158.431, 82.539 |
| Unit cell angles | 90.00, 90.11, 90.00 |
Refinement procedure
| Resolution | 37.240 - 3.100 |
| R-factor | 0.31803 |
| Rwork | 0.314 |
| R-free | 0.39658 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3m17 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.184 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.200 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Number of reflections | 29051 | |
| Completeness [%] | 90.4 | 58 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 294 | 2ul protein:peptide with 2ul buffer containing 100 mM phosphate/citric acid, 22% PEG 1000 and 8% ethanol , pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 294K |
