5U12
E. coli dihydropteroate synthase complexed with an 8-mercaptoguanine derivative: 2-azanyl-8-[(2-fluorophenyl)methylsulfanyl]-1,9-dihydropurin-6-one
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-04-07 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.95370 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 95.887, 84.546, 84.145 |
Unit cell angles | 90.00, 109.87, 90.00 |
Refinement procedure
Resolution | 45.089 - 1.839 |
R-factor | 0.181 |
Rwork | 0.180 |
R-free | 0.20460 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1aj2 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.284 |
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] | 46.570 | 1.880 |
High resolution limit [Å] | 1.839 | 1.840 |
Rmerge | 0.060 | 0.649 |
Number of reflections | 54783 | |
<I/σ(I)> | 18.6 | 2.8 |
Completeness [%] | 99.7 | 97 |
Redundancy | 7.4 | 7.2 |
CC(1/2) | 0.999 | 0.872 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.8 | 281 | 0.147M magnesium acetate 27.1% [w/v] MPEG 5000 0.1M tris chloride, pH 8.8 Protein at 11.1 mg.mL-1 Cocrystallisation 1:1 (150:150 nL) reservoir:protein |