2W12
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 | 38.000, 59.500, 81.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 17.770 - 1.460 |
R-factor | 0.149 |
Rwork | 0.148 |
R-free | 0.17800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nd1 |
RMSD bond length | 0.018 |
RMSD bond angle | 1.861 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.300 | 1.550 |
High resolution limit [Å] | 1.460 | 1.460 |
Rmerge | 0.060 | 0.250 |
Number of reflections | 32970 | |
<I/σ(I)> | 21.9 | 6.7 |
Completeness [%] | 98.4 | 90.1 |
Redundancy | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | PEG 2000, TRIS, pH 6.5 |