3LV8
1.8 Angstrom resolution crystal structure of a thymidylate kinase (tmk) from Vibrio cholerae O1 biovar eltor str. N16961 in complex with TMP, thymidine-5'-diphosphate and ADP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-02-10 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 43 3 2 |
| Unit cell lengths | 112.973, 112.973, 112.973 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.800 |
| R-factor | 0.16611 |
| Rwork | 0.164 |
| R-free | 0.20393 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4tmk |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.494 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.071 | 0.426 |
| Number of reflections | 23299 | |
| <I/σ(I)> | 28.3 | 3.8 |
| Completeness [%] | 99.5 | 95.3 |
| Redundancy | 10 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 295 | 7mg/mL protein; The PACT Suite condition #47 (D11), pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
