1GKF
Crystal structures of penicillin acylase enzyme-substrate complexes: Structural insights into the catalytic mechanism
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MAR scanner 300 mm plate |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 51.200, 131.700, 63.900 |
Unit cell angles | 90.00, 105.70, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.410 |
R-factor | 0.149 * |
Rwork | 0.148 |
R-free | 0.16900 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 * |
RMSD bond angle | 0.026 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.430 |
High resolution limit [Å] | 1.400 | 1.410 |
Rmerge | 0.052 | 0.176 |
Total number of observations | 361905 * | |
Number of reflections | 152163 | |
<I/σ(I)> | 19.8 | 4.4 |
Completeness [%] | 97.4 | 95.9 * |
Redundancy | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.2 * | 291 * | McVey, C.E., (1997) Acta Crystallog., D53, 777. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | MOPS | 50 (mM) | pH7.2 |
3 | 1 | reservoir | MOPS | 50 (mM) | pH7.2 |
4 | 1 | reservoir | PEG2000 MME | 10-12 (%) | |
5 | 1 | reservoir | ethylene glycol | 20-25 (%) |