2W15
High-resolution crystal structure of the P-I snake venom metalloproteinase BaP1 in complex with a peptidomimetic: insights into inhibitor binding
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 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.900, 59.800, 83.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.670 - 1.050 |
R-factor | 0.117 |
Rwork | 0.116 |
R-free | 0.14300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2w14 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.793 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.110 |
High resolution limit [Å] | 1.050 | 1.050 |
Rmerge | 0.050 | 0.220 |
Number of reflections | 84722 | |
<I/σ(I)> | 25.2 | 7.8 |
Completeness [%] | 95.0 | 75.9 |
Redundancy | 7.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | PEG 3000, HEPES, NACL, pH 7.5 |