5CKU
Structure of Aspergillus fumigatus ornithine hydroxylase (SidA) mutant N323A bound to NADP and ornithine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-07-25 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.979180 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 77.081, 84.002, 145.057 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 72.690 - 2.100 |
R-factor | 0.1752 |
Rwork | 0.172 |
R-free | 0.22810 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 4b63 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.036 |
Data reduction software | XDS |
Data scaling software | Aimless (0.3.6) |
Phasing software | PHENIX |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 72.690 | 72.690 | 2.160 |
High resolution limit [Å] | 2.100 | 8.910 | 2.100 |
Rmerge | 0.131 | 0.050 | 0.617 |
Rpim | 0.058 | 0.022 | 0.280 |
Total number of observations | 156743 | 2095 | 12377 |
Number of reflections | 27670 | ||
<I/σ(I)> | 9.3 | 22.6 | 2.7 |
Completeness [%] | 99.6 | 94.4 | 100 |
Redundancy | 5.7 | 5.5 | 5.6 |
CC(1/2) | 0.994 | 0.997 | 0.861 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.6 | 293 | 0.1 M HEPES, pH 6.6, 1.86 M ammonium sulfate, and 1% (v/v) dioxane. Protein stock solution contained 8 mg/mL enzyme with 1 mM NADP+ and 100 mM L-ornithine. |