5NNR
Structure of Naa15/Naa10 bound to HypK-THB
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-10-28 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.978333 |
Spacegroup name | P 32 |
Unit cell lengths | 85.348, 85.348, 319.626 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 42.299 - 3.100 |
R-factor | 0.2318 |
Rwork | 0.230 |
R-free | 0.27170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5nnp |
RMSD bond length | 0.009 |
RMSD bond angle | 1.452 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.350 | 3.210 |
High resolution limit [Å] | 3.100 | 3.100 |
Rpim | 0.065 | 0.977 |
Number of reflections | 47332 | 4684 |
<I/σ(I)> | 13.8 | 1.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 11.7 | 11.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | 0.2 M Mg(NO3)2 20% PEG 3350 protein concentration 25 - 30 mg/ml |