5NZ5
A C145S mutant of Nesterenkonia AN1 amidase from the nitrilase superfamily
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-11-14 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.8856 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 75.399, 114.996, 65.589 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 22.990 - 1.470 |
R-factor | 0.1417 |
Rwork | 0.141 |
R-free | 0.16320 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3hkx |
RMSD bond length | 0.029 |
RMSD bond angle | 2.561 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.15) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 23.646 | 23.646 | 1.550 |
High resolution limit [Å] | 1.470 | 4.650 | 1.470 |
Rmerge | 0.024 | 0.375 | |
Rmeas | 0.071 | 0.026 | 0.407 |
Rpim | 0.027 | 0.010 | 0.155 |
Total number of observations | 337984 | 11024 | 47000 |
Number of reflections | 48675 | ||
<I/σ(I)> | 17 | 42.7 | 4.5 |
Completeness [%] | 99.9 | 98.7 | 99.9 |
Redundancy | 6.9 | 6.7 | 6.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | 0.2M Ammonium sulfate, 0.1M Sodium cacodylate trihydtrate, 30% PEG 8000 |