4HPX
Crystal structure of Tryptophan Synthase at 1.65 A resolution in complex with alpha aminoacrylate E(A-A) and benzimidazole in the beta site and the F9 inhibitor in the alpha 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 | 2011-12-31 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 183.960, 60.960, 67.410 |
Unit cell angles | 90.00, 94.58, 90.00 |
Refinement procedure
Resolution | 28.190 - 1.650 |
R-factor | 0.1445 |
Rwork | 0.142 |
R-free | 0.19010 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tjp |
RMSD bond length | 0.010 |
RMSD bond angle | 1.427 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.16) |
Phasing software | PHASER (2.1.4) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 91.686 | 29.376 | 1.740 |
High resolution limit [Å] | 1.650 | 5.220 | 1.650 |
Rmerge | 0.034 | 0.330 | |
Total number of observations | 10674 | 44289 | |
Number of reflections | 87817 | ||
<I/σ(I)> | 10.8 | 18 | 2.3 |
Completeness [%] | 98.3 | 99.5 | 96.2 |
Redundancy | 3.6 | 3.6 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 298 | 50 mM Bicine-CsOH, 10% PEG 8000, 2 mM Spermine, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |