2REF
Crystal structure of the loading GNATL domain of CurA from Lyngbya majuscula soaked with malonyl-CoA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-06-06 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97939 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 91.886, 91.886, 139.486 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 46.500 - 2.750 |
R-factor | 0.21 |
Rwork | 0.207 |
R-free | 0.25100 |
Starting model (for MR) | Apo CurA GNATL domain |
RMSD bond length | 0.008 |
RMSD bond angle | 1.351 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.500 | 2.850 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.094 | 0.534 |
Number of reflections | 18214 | |
<I/σ(I)> | 10.6 | 4.9 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 9.7 | 9.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 277.15 | Mother liquor: 100 mM Bis-Tris pH 6.8, 100 mM NaCl, 1.5 M ammonium sulfate, 20% glycerol. Protein buffer: 20 mM Tris pH 7.9, 500 mM NaCl, 10% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K |