9M2Y
Crystal structure of a DUF3237 protein from Aspergillus
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL10U2 |
| Synchrotron site | SSRF |
| Beamline | BL10U2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-01-19 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9793 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 45.360, 70.911, 90.204 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.680 - 1.560 |
| R-factor | 0.1747 |
| Rwork | 0.173 |
| R-free | 0.18990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.234 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.21)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 90.200 | 1.590 |
| High resolution limit [Å] | 1.560 | 1.560 |
| Rmerge | 0.031 | 0.711 |
| Rmeas | 0.033 | 0.774 |
| Rpim | 0.010 | 0.296 |
| Total number of observations | 232997 | 6440 |
| Number of reflections | 21058 | 971 |
| <I/σ(I)> | 33.7 | 2.7 |
| Completeness [%] | 99.8 | |
| Redundancy | 11.1 | 6.6 |
| CC(1/2) | 1.000 | 0.891 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 288.2 | 0.2 M Ammonium acetate, 0.1M Sodium acetate trihydrate, plus 30% PEG4000 |
