5CDE
R372A mutant of Xaa-Pro dipeptidase from Xanthomonas campestris
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | RRCAT INDUS-2 BEAMLINE PX-BL21 |
Synchrotron site | RRCAT INDUS-2 |
Beamline | PX-BL21 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-04-13 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.28225 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 81.088, 101.947, 111.509 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.921 - 1.850 |
R-factor | 0.1866 |
Rwork | 0.185 |
R-free | 0.22420 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.097 |
Data scaling software | Aimless (0.5.7) |
Phasing software | RESOLVE |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 46.360 | 46.360 | 1.890 |
High resolution limit [Å] | 1.850 | 9.430 | 1.850 |
Rmerge | 0.073 | 0.033 | 0.686 |
Rpim | 0.030 | 0.014 | 0.319 |
Total number of observations | 539390 | 4027 | 19647 |
Number of reflections | 77891 | ||
<I/σ(I)> | 20.1 | 54 | 2.1 |
Completeness [%] | 98.0 | 97.7 | 79.8 |
Redundancy | 6.9 | 5.9 | 5.5 |
CC(1/2) | 0.999 | 0.999 | 0.800 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 5.5 | 294 | 0.1 M BisTris pH 5.5, 0.2 M Lithium sulphate, 25 % PEG 3350, 1 mM ZnCl2 |