3K3T
E185A mutant of peptidoglycan hydrolase 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 |
Collection date | 2009-04-09 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 54.441, 54.441, 101.569 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 26.290 - 1.750 |
R-factor | 0.1994 |
Rwork | 0.198 |
R-free | 0.22848 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2zyc |
RMSD bond length | 0.006 |
RMSD bond angle | 0.874 |
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 | 1.810 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.070 | 0.365 |
Number of reflections | 16152 | |
Completeness [%] | 99.7 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 100mM MES pH 6.0, 1.9M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |