5SUH
The structure of double ringed trimeric shell protein MSM0271 from the RMM microcompartment
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-10 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97949 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 139.890, 139.890, 150.120 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.139 - 2.700 |
R-factor | 0.1755 |
Rwork | 0.173 |
R-free | 0.22430 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MSM0275 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.278 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.200 | 2.770 |
High resolution limit [Å] | 2.700 | 2.700 |
Number of reflections | 24387 | |
<I/σ(I)> | 19.2 | 2.1 |
Completeness [%] | 99.9 | 100 |
Redundancy | 9.6 | 11.1 |
CC(1/2) | 0.997 | 0.752 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 10 mg/mL protein, 0.8 M Na/K tartrate, 0.1 M Tris, 0.5% (w/v) PEG 2000MME |