3AMJ
The crystal structure of the heterodimer of M16B peptidase from Sphingomonas sp. A1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 67.457, 100.676, 253.770 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.760 - 3.000 |
R-factor | 0.21486 |
Rwork | 0.210 |
R-free | 0.30046 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3gwd |
RMSD bond length | 0.009 |
RMSD bond angle | 1.014 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.124 | 0.365 |
Number of reflections | 35597 | |
<I/σ(I)> | 23.79 | 7.7 |
Completeness [%] | 99.9 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.6 | 293 | 10% PDG 8000, 0.1M Tris-HCl, pH 8.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |