5XHQ
Apolipoprotein N-acyl Transferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U1 |
Synchrotron site | SSRF |
Beamline | BL17U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-08-08 |
Detector | DECTRIS PILATUS 300K |
Wavelength(s) | 0.9793 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 90.869, 134.094, 135.159 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.364 - 2.587 |
R-factor | 0.2355 |
Rwork | 0.233 |
R-free | 0.28770 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ems |
RMSD bond length | 0.013 |
RMSD bond angle | 1.549 |
Data reduction software | HKL-2000 (2.2.0) |
Data scaling software | HKL-2000 (2.2.0) |
Phasing software | PHENIX (dev_1819) |
Refinement software | PHENIX (dev_1819) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.400 | 2.640 |
High resolution limit [Å] | 2.587 | 2.600 |
Rmerge | 0.135 | 0.665 |
Number of reflections | 51623 | 1457 |
<I/σ(I)> | 14.8 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.2 | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 289 | 50 mM Tris-HCl (pH 7.5) and 26% (v/v) PEG 550 MME |