1FFL
CRYSTAL STRUCTURE OF THE APO-THYMIDYLATE SYNTHASE R166Q MUTANT
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR571 |
| Temperature [K] | 298 |
| Detector technology | DIFFRACTOMETER |
| Collection date | 1997-05-04 |
| Detector | ENRAF-NONIUS FAST |
| Spacegroup name | I 21 3 |
| Unit cell lengths | 132.500, 132.500, 132.500 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.130 - 2.940 |
| R-factor | 0.17 * |
| Rwork | 0.171 |
| R-free | 0.21000 * |
| Structure solution method | Fourier Difference Maps |
| Starting model (for MR) | Wildtype Binary Complex of E.coli thymidylate synthase |
| RMSD bond length | 0.008 * |
| RMSD bond angle | 1.400 * |
| Data reduction software | MADNESS |
| Data scaling software | CCP4 ((AGROVATA) |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.000 * | 3.020 |
| High resolution limit [Å] | 2.940 | 2.940 |
| Rmerge | 0.090 | 0.380 |
| Number of reflections | 8138 | |
| <I/σ(I)> | 7.4 | |
| Completeness [%] | 96.0 * | 96 |
| Redundancy | 7 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8 * | 298 | Montfort, W.R., (1990) Biochemistry, 29, 6964. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5-9 (mg/mL) | |
| 2 | 1 | drop | potasssium | 20 (mM) | |
| 3 | 1 | drop | ammonium | 2.3 (M) | |
| 4 | 1 | drop | dUMP | 100 (mM) | |
| 5 | 1 | drop | CB3717 | 4.78 (mM) | |
| 6 | 1 | reservoir | potassium | 20 (mM) | |
| 7 | 1 | reservoir | disodium ethylenediaminetetraacetic acid | 0.1 (mM) | |
| 8 | 1 | reservoir | beta-mercaptoethanol | 20 (mM) |
