4DLF
Crystal structure of an amidohydrolase (COG3618) from burkholderia multivorans (TARGET EFI-500235) with bound ZN, space group P3221
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-10-15 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9793 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 75.300, 75.300, 142.450 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.386 - 1.925 |
R-factor | 0.1944 |
Rwork | 0.193 |
R-free | 0.22820 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4dnm |
RMSD bond length | 0.012 |
RMSD bond angle | 1.082 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.16) |
Phasing software | PHENIX |
Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 65.212 | 38.386 | 2.030 |
High resolution limit [Å] | 1.925 | 6.090 | 1.920 |
Rmerge | 0.021 | 0.021 | |
Total number of observations | 7068 | 29620 | |
Number of reflections | 36087 | ||
<I/σ(I)> | 7.3 | 10.5 | 0.4 |
Completeness [%] | 99.8 | 98.3 | 99.9 |
Redundancy | 5.9 | 5.7 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | sitting drop vapor diffuction | 7.5 | 298 | Protein (10 mM Hepes, pH 7.8, 150 mM NaCl, 10% glycerol, 0.5 mM ZnCl, 0.5 mM D-arabonate-1,4-lactone; Reservoir (20% Peg3350, 100 mM HEPES pH 7.5); Cryoprotection (Reservoir, 5 mM Zn, 25 mM D-arabonate-1,4-lactone, 20% glycerol), sitting drop vapor diffuction, temperature 298K |