4R3L
Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus bound to substrate peptide fragment and CoA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL15A |
Synchrotron site | NSRRC |
Beamline | BL15A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-07-28 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 35.185, 58.004, 84.109 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.875 - 1.839 |
R-factor | 0.1957 |
Rwork | 0.190 |
R-free | 0.24540 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2x7b |
RMSD bond length | 0.007 |
RMSD bond angle | 1.090 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | BALBES |
Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 1.839 |
Rmerge | 0.044 |
Number of reflections | 15532 |
Completeness [%] | 99.8 |
Redundancy | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 283 | 12.5% PEG 4000, 0.1M sodium acetate trihydrate pH 4.2, 0.1M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 283K |