4HST
Crystal structure of a double mutant of a class III engineered cephalosporin acylase
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-03-28 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.95663 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 68.385, 77.845, 191.990 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 95.995 - 1.571 |
R-factor | 0.12145 |
Rwork | 0.119 |
R-free | 0.16225 |
Structure solution method | MAD |
RMSD bond length | 0.027 |
RMSD bond angle | 2.220 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELXS |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 95.995 |
High resolution limit [Å] | 1.571 |
Rmerge | 0.095 |
Number of reflections | 133919 |
<I/σ(I)> | 16.1 |
Completeness [%] | 93.7 |
Redundancy | 12 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 10-20% PEG8000, 10 mM Tris-HCl, pH 8.0-8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |