3M17
Crystal structure of human FcRn with a monomeric peptide inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Collection date | 2007-09-01 |
Wavelength(s) | 1.0 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 114.320, 118.300, 248.330 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.100 - 2.600 |
R-factor | 0.26408 |
Rwork | 0.261 |
R-free | 0.32548 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1exu |
RMSD bond length | 0.006 |
RMSD bond angle | 0.962 |
Data reduction software | d*TREK |
Data scaling software | d*TREK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.100 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 51434 | |
Completeness [%] | 98.7 | 97.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |