6VNT
Tryptophan synthase in complex with inhibitor N-(4'-trifluoromethoxybenzenesulfonyl)-2-amino-1-ethylphosphate (F9F) at the alpha-site, aminoacrylate at the beta site, and sodium ion at the metal coordination site at 1.25 Angstrom resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 12.3.1 |
Synchrotron site | ALS |
Beamline | 12.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-08-14 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.000014 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 183.022, 59.382, 67.322 |
Unit cell angles | 90.00, 94.92, 90.00 |
Refinement procedure
Resolution | 36.310 - 1.250 |
R-factor | 0.154 |
Rwork | 0.153 |
R-free | 0.18070 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4hn4 |
RMSD bond length | 0.004 |
RMSD bond angle | 1.215 |
Data reduction software | MOSFLM (7.2.2) |
Data scaling software | SCALA (3.3.22) |
Phasing software | PHASER (2.8.3) |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 91.174 | 36.285 | 1.320 |
High resolution limit [Å] | 1.250 | 3.950 | 1.251 |
Rmerge | 0.043 | 0.707 | |
Rmeas | 0.099 | 0.047 | 0.836 |
Rpim | 0.033 | 0.016 | 0.442 |
Number of reflections | 187530 | 6325 | 25029 |
<I/σ(I)> | 10.8 | 14.6 | 1 |
Completeness [%] | 94.9 | 98 | 87 |
Redundancy | 7.3 | 8.8 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 293 | 50 mM Bicine-NaOH, 10% PEG 8,000, 2 mM Spermine, pH 7.8 |