5U14
E. coli dihydropteroate synthase complexed with an 8-mercaptoguanine derivative: 4-{2-[(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl]ethyl}benzene-1-sulfonamide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-10-22 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.95370 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 94.828, 85.101, 84.073 |
Unit cell angles | 90.00, 111.15, 90.00 |
Refinement procedure
Resolution | 36.618 - 1.953 |
R-factor | 0.2098 |
Rwork | 0.207 |
R-free | 0.25670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1aj2 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.303 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.328 | 1.990 |
High resolution limit [Å] | 1.941 | 1.941 |
Rmerge | 0.039 | 0.683 |
Number of reflections | 45137 | |
<I/σ(I)> | 29.3 | 2.6 |
Completeness [%] | 97.9 | 69.2 |
Redundancy | 7.4 | 7.1 |
CC(1/2) | 1.000 | 0.884 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.7 | 281 | 0.156 M magnesium chloride 28.6% [w/v] MPEG 5000 0.1 M tris chloride, pH 7.7 Protein at 11.1 mg.mL-1 Cocrystallisation 1:1 (150:150 nL) reservoir:protein |