7OVU
Crystal structure of Arabidopsis thaliana NAT9 in complex with AcCoA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-12-14 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.976251 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 67.202, 48.895, 60.123 |
Unit cell angles | 90.00, 102.75, 90.00 |
Refinement procedure
Resolution | 39.190 - 1.450 |
R-factor | 0.1502 |
Rwork | 0.149 |
R-free | 0.18090 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3eo4 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.190 | 1.500 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.072 | |
Number of reflections | 33777 | 3306 |
<I/σ(I)> | 15.9 | 1.2 |
Completeness [%] | 99.7 | |
Redundancy | 13.1 | |
CC(1/2) | 1.000 | 0.509 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | AtNAT9 was concentrated to 15 mg/ml and incubated with a threefold molar excess of AcCoA for 18 h on ice. Crystallization drops contained 200 nl protein solution and 200 nl precipitant solution (0.1 M HEPES (pH 7) and 20 % PEG6000) and crystals appeared after seven days. The crystals were cryo-protected with 20 % glycerol and flash-frozen in liquid nitrogen. |