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 |
