3GOV
Crystal structure of the catalytic region of human MASP-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-11-01 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 0.8148 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 68.418, 70.412, 121.413 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.980 - 2.550 |
R-factor | 0.231 |
Rwork | 0.229 |
R-free | 0.27800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MASP-1 serine protease domain(unpublished) CCP1 and CCP2 modules of PDB entry 1zjk |
RMSD bond length | 0.007 |
RMSD bond angle | 1.163 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.980 | 2.600 |
High resolution limit [Å] | 2.550 | 2.550 |
Rmerge | 0.095 | 0.472 |
Number of reflections | 19349 | 1066 |
<I/σ(I)> | 15.96 | 4.3 |
Completeness [%] | 97.9 | 97.4 |
Redundancy | 5.9 | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | well solution: 11%(w/v) PEG3350, 0.1 M MES; protein solution: 50 mM NaCl, 5 mM Tris, 0.5 mM EDTA, 20 mM benzamidine-HCl, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |