5KD2
BT_4244 metallopeptidase from Bacteroides thetaiotaomicron
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-07-03 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97945 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 81.957, 81.957, 182.138 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 70.980 - 2.150 |
R-factor | 0.17077 |
Rwork | 0.169 |
R-free | 0.20984 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.528 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.980 | 2.220 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.070 | 0.366 |
Number of reflections | 39361 | |
<I/σ(I)> | 15.9 | 4.1 |
Completeness [%] | 99.9 | 100 |
Redundancy | 6.5 | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | PEG 3350, K/Na Tartrate, Tris-HCl pH 8.0 |