3EEV
Crystal Structure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-08-11 |
| Detector | SBC-3 |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 99.972, 99.972, 127.374 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 32.700 - 2.610 |
| R-factor | 0.178 |
| Rwork | 0.175 |
| R-free | 0.24200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2xat |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.606 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.5.0053) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.700 | 2.640 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.103 | 0.660 |
| Number of reflections | 22994 | |
| <I/σ(I)> | 5.1 | 2.5 |
| Completeness [%] | 99.8 | 99.6 |
| Redundancy | 9.7 | 9.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 295 | 0.2 M Ammonium phosphate, 0.1 M TRIS pH 8.5, 50 %v/v MPD, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
