3JTR
Mutations in Cephalosporin Acylase Affecting Stability and Autoproteolysis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 4A |
Synchrotron site | PAL/PLS |
Beamline | 4A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-04-29 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.00000 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 73.816, 73.816, 381.324 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.500 - 2.500 |
R-factor | 0.184 |
Rwork | 0.182 |
R-free | 0.22400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2adv |
RMSD bond length | 0.012 |
RMSD bond angle | 1.312 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.070 | 0.160 |
Number of reflections | 34291 | |
<I/σ(I)> | 24.3 | 12.7 |
Completeness [%] | 90.3 | 79.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | 0.1M Na-cacodylate (pH 6.5), 0.2M magnesium chloride, PEG 3000, VAPOR DIFFUSION, HANGING DROP, temperature 295K |