3KJR
Crystal structure of dihydrofolate reductase/thymidylate synthase from Babesia bovis determined using SlipChip based microfluidics
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-07-27 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0332 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 83.113, 97.559, 152.830 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.950 |
| R-factor | 0.17025 |
| Rwork | 0.169 |
| R-free | 0.20112 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDBid:3I3R |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.356 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.073 | 0.470 |
| Number of reflections | 89311 | |
| <I/σ(I)> | 14 | 2.1 |
| Completeness [%] | 98.2 | 98.4 |
| Redundancy | 2.8 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | SlipChip based Microbatch | 9.5 | 296 | a protein sample was mixed at 1:2 ratio with 20 % (w/v) PEG-8000, 0.2 M NaCl and 0.1 M CHES, pH 9.5, SlipChip based Microbatch, temperature 296K |
