8ODO
Structure of human guanylylated RTCB in complex with Archease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-09-03 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.9737 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 99.090, 125.547, 125.733 |
| Unit cell angles | 90.00, 108.51, 90.00 |
Refinement procedure
| Resolution | 75.230 - 2.200 |
| R-factor | 0.1945 |
| Rwork | 0.193 |
| R-free | 0.21760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | D_1292120363 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.496 |
| Data reduction software | XDS (20210205) |
| Data scaling software | Aimless (1.12.10) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 119.230 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.110 | 1.160 |
| Rpim | 0.045 | 0.495 |
| Number of reflections | 145859 | 6868 |
| <I/σ(I)> | 9.2 | 1.1 |
| Completeness [%] | 99.3 | 95.2 |
| Redundancy | 7 | 6.3 |
| CC(1/2) | 0.998 | 0.860 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291.15 | protein: RTCB 160 uM, Archease 200 uM, 2 mM manganese chloride, 2 mM GTP reservoir: 10% w/v PEG 8000, 0.1 M HEPES pH 7.5, 8% v/v ethylene glycol drop: 200 nl protein + 200 nl reservoir |
