5U11
E. coli dihydropteroate synthase complexed with an 8-mercaptoguanine derivative: 2-[(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl]-N-methylacetamide
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 | 2016-04-15 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.95370 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 94.782, 84.599, 83.963 |
Unit cell angles | 90.00, 110.52, 90.00 |
Refinement procedure
Resolution | 37.252 - 1.994 |
R-factor | 0.2 |
Rwork | 0.198 |
R-free | 0.23030 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1aj2 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.335 |
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] | 46.200 | 2.040 |
High resolution limit [Å] | 1.990 | 1.990 |
Rmerge | 0.067 | 0.726 |
Number of reflections | 42177 | |
<I/σ(I)> | 14.8 | 2 |
Completeness [%] | 98.6 | 81.7 |
Redundancy | 7.4 | 7.1 |
CC(1/2) | 0.999 | 0.848 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 281 | 0.083 M magnesium sulfate 24.5% [w/v] PEG6000 0.1 M sodium cacodylate, pH 6.32 Protein at 11.1 mg.mL-1 Cocrystallisation 1:1 (150:150 nL) reservoir:protein |