9AZH
Native nnhA in P1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-08-08 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.18157 |
| Spacegroup name | P 1 |
| Unit cell lengths | 59.727, 117.377, 121.125 |
| Unit cell angles | 117.14, 91.30, 101.38 |
Refinement procedure
| Resolution | 54.090 - 2.040 |
| Rwork | 0.156 |
| R-free | 0.17850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.546 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 60.740 | 2.070 |
| High resolution limit [Å] | 2.040 | 2.040 |
| Rmerge | 0.222 | 0.843 |
| Rpim | 0.090 | 0.390 |
| Number of reflections | 177958 | 8535 |
| <I/σ(I)> | 9.6 | 2.2 |
| Completeness [%] | 98.2 | 94.6 |
| Redundancy | 7 | 5.3 |
| CC(1/2) | 0.987 | 0.696 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 293 | Protein at 7mg/mL was set up in SD2 sitting drop plates with 300 nL protein and 150 nL reservoir at 20 C. Reservoir consisted of 21% polyacrylic acid 5100, 20 mM MgCl2 and 100 mM HEPES at pH 7.2 |
