1GHP
STRUCTURES OF THE ACYL-ENZYME COMPLEX OF THE STAPHYLOCOCCUS AUREUS BETA-LACTAMASE MUTANT GLU166ASP:ASN170GLN WITH DEGRADED BENZYLPENICILLIN
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 | 1998-01-15 |
| Detector | BRANDEIS - B1 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 52.900, 89.700, 138.800 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.760 |
| R-factor | 0.185 |
| Rwork | 0.185 |
| R-free | 0.26400 |
| Structure solution method | OTHER |
| Starting model (for MR) | 1djc |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.900 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | X-PLOR (3.7) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 21.800 | 1.820 |
| High resolution limit [Å] | 1.760 | 1.760 |
| Rmerge | 0.053 | 0.109 |
| Number of reflections | 29494 | 2061 * |
| <I/σ(I)> | 17.9 | 2.2 |
| Completeness [%] | 86.6 | 63 |
| Redundancy | 2.8 | 2.78 |
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) |
