3AMI
The crystal structure of the M16B metallopeptidase subunit 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 1 21 1 |
Unit cell lengths | 50.405, 139.757, 63.714 |
Unit cell angles | 90.00, 107.91, 90.00 |
Refinement procedure
Resolution | 42.780 - 2.400 |
R-factor | 0.19982 |
Rwork | 0.196 |
R-free | 0.26586 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 0.962 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.133 | 0.356 |
Number of reflections | 32754 | |
<I/σ(I)> | 18.33 | 4.47 |
Completeness [%] | 100.0 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 293 | 12% PEG 4000, 0.1M litium sulfate, 0.1M sodium citrate, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |