6VFD
Tryptophan synthase mutant Q114A in complex with cesium ion at the metal coordination site and 2-aminophenol quinonoid at the enzyme beta site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2018-09-28 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 183.079, 59.340, 67.440 |
| Unit cell angles | 90.00, 94.85, 90.00 |
Refinement procedure
| Resolution | 29.690 - 1.700 |
| R-factor | 0.1959 |
| Rwork | 0.195 |
| R-free | 0.22370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hpj |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.285 |
| Data reduction software | MOSFLM (7.2.2) |
| Data scaling software | SCALA (3.3.22) |
| Phasing software | MOLREP (7.0.078) |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 91.212 | 36.898 | 1.690 |
| High resolution limit [Å] | 1.600 | 5.060 | 1.600 |
| Rmerge | 0.049 | 0.360 | |
| Rmeas | 0.077 | 0.057 | 0.436 |
| Rpim | 0.040 | 0.030 | 0.242 |
| Total number of observations | 316674 | 11051 | 39804 |
| Number of reflections | 93786 | 3130 | 12618 |
| <I/σ(I)> | 8.7 | 20.3 | 2 |
| Completeness [%] | 98.5 | 99.7 | 91 |
| Redundancy | 3.4 | 3.5 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 293 | 50 mM Bicine-CsOH, 10% PEG 8,000, 4 mM spermine |
