1GHM
Structures of the acyl-enzyme complex of the staphylococcus aureus beta-lactamase mutant GLU166ASP:ASN170GLN with degraded cephaloridine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-10-15 |
Detector | BRANDEIS - B4 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 53.500, 90.800, 140.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 21.800 - 1.860 |
R-factor | 0.188 |
Rwork | 0.188 |
R-free | 0.24100 |
Starting model (for MR) | 1djc |
RMSD bond length | 0.020 |
RMSD bond angle | 1.900 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | CNS (0.4) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 21.800 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.045 | 0.413 |
Number of reflections | 31672 | 3077 * |
<I/σ(I)> | 16.7 | 1.6 |
Completeness [%] | 98.4 | 96.9 |
Redundancy | 3.1 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | enzyme | 10 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 89 (%sat) | |
3 | 1 | reservoir | PEG2000 | 0.5 (%) | |
4 | 1 | reservoir | sodium bicarbonate | 0.1 (M) |