3LN9
Crystal structure of the fibril-specific B10 antibody fragment
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 | 2009-02-05 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9184 |
Spacegroup name | P 2 3 |
Unit cell lengths | 84.124, 84.124, 84.124 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 18.800 - 1.800 |
R-factor | 0.19876 |
Rwork | 0.197 |
R-free | 0.23295 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ol0 |
RMSD bond length | 0.020 |
RMSD bond angle | 1.918 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.4.0062) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.057 | 0.624 |
Number of reflections | 19838 | |
<I/σ(I)> | 21.05 | 3.1 |
Completeness [%] | 99.8 | 100 |
Redundancy | 5.5 | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.7 | 288 | 200mM Sodium Citrate, 2M Ammonium Sulphate, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 288K |