6X0C
Tryptophan Synthase mutant beta-Q114A in complex with Cesium ion at the metal coordination site and aminoacrylate and benzimidazole at the enzyme beta site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-03-28 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.979200 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 183.133, 59.336, 67.419 |
Unit cell angles | 90.00, 95.11, 90.00 |
Refinement procedure
Resolution | 39.390 - 1.450 |
R-factor | 0.1656 |
Rwork | 0.164 |
R-free | 0.20200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6vfd |
RMSD bond length | 0.009 |
RMSD bond angle | 1.570 |
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] | 40.000 | 39.391 | 1.530 |
High resolution limit [Å] | 1.450 | 4.590 | 1.450 |
Rmerge | 0.104 | 0.077 | 1.103 |
Rmeas | 0.111 | 0.082 | 1.173 |
Rpim | 0.030 | 0.022 | 0.323 |
Total number of observations | 53693 | 240545 | |
Number of reflections | 127033 | 4171 | 18507 |
<I/σ(I)> | 13.7 | 34.1 | 3.8 |
Completeness [%] | 100.0 | 99.8 | 99.9 |
Redundancy | 13.3 | 12.9 | 13 |
CC(1/2) | 0.998 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 298 | 50 mM Bicine-CsOH, 10% PEG 8,000, 2 mM Spermine, pH 7.8 |