5IMH
D31P mutant of C69-family cysteine dipeptidase from Lactobacillus farciminis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-01-17 |
Detector | RIGAKU SATURN A200 |
Wavelength(s) | 1.00 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 192.337, 137.088, 101.297 |
Unit cell angles | 90.00, 100.75, 90.00 |
Refinement procedure
Resolution | 47.240 - 2.471 |
R-factor | 0.1904 |
Rwork | 0.188 |
R-free | 0.24050 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5iau |
RMSD bond length | 0.011 |
RMSD bond angle | 1.807 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.240 | 2.510 |
High resolution limit [Å] | 2.470 | 2.470 |
Rmerge | 0.098 | 0.351 |
Number of reflections | 91739 | |
<I/σ(I)> | 44.92 | 7.645 |
Completeness [%] | 99.5 | 98.8 |
Redundancy | 7.3 | 6.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 1.0 M 1,6-hexanediol, 10 mM CoCl2, 100 mM acetate |