9M2Z
Crystal structure of an DUF3237 protein from Aspergillus
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 | 45.100, 70.520, 88.850 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.870 - 1.720 |
| R-factor | 0.1826 |
| Rwork | 0.182 |
| R-free | 0.19750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.350 |
| 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] | 29.620 | 1.760 |
| High resolution limit [Å] | 1.720 | 1.720 |
| Rmerge | 0.045 | 0.396 |
| Rmeas | 0.048 | 0.437 |
| Rpim | 0.014 | 0.181 |
| Total number of observations | 151900 | 5605 |
| Number of reflections | 15324 | 1039 |
| <I/σ(I)> | 29 | 5.2 |
| Completeness [%] | 99.3 | |
| Redundancy | 9.9 | 5.4 |
| CC(1/2) | 0.999 | 0.924 |
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, 30% PEG4000 |
