1QLR
CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF A HUMAN MONOCLONAL IgM COLD AGGLUTININ
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LNLS BEAMLINE D03B-MX1 |
Synchrotron site | LNLS |
Beamline | D03B-MX1 |
Temperature [K] | 291 |
Detector technology | IMAGE PLATE |
Collection date | 1998-02-15 |
Detector | MARRESEARCH |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 115.660, 115.660, 174.950 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 13.100 - 2.830 |
R-factor | 0.216 * |
Rwork | 0.216 |
R-free | 0.26500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dfb |
RMSD bond length | 0.014 |
RMSD bond angle | 0.047 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 13.100 | 2.890 |
High resolution limit [Å] | 2.830 | 2.830 |
Rmerge | 0.069 | |
Number of reflections | 31329 | |
Completeness [%] | 96.8 | 99 * |
Redundancy | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 25 * | Cauerhff, A., (1998) Protein Pept.Lett., 5, 177. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | PEG8000 | 14 (%(w/w)) | |
3 | 1 | reservoir | sodium HEPES | 0.1 (M) |