5L03
Crystal structure of 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE Synthase from BURKHOLDERIA PSEUDOMALLEI bound to L-tryptophan hydroxamate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 80 |
Detector technology | CCD |
Collection date | 2015-03-25 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.00 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 116.515, 68.126, 60.659 |
Unit cell angles | 90.00, 96.93, 90.00 |
Refinement procedure
Resolution | 30.714 - 1.469 |
R-factor | 0.1798 |
Rwork | 0.179 |
R-free | 0.19950 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 0.919 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | REFMAC |
Refinement software | PHENIX (1.10_2142) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.721 |
High resolution limit [Å] | 1.469 |
Number of reflections | 79230 |
<I/σ(I)> | 19.9 |
Completeness [%] | 99.0 |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 292 | Tris,NaCl, PEG 4000, ZnCl2 |