5HAT
Structure function studies of R. palustris RubisCO (S59F/M331A mutant; CABP-bound)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-11-07 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.9790 |
Spacegroup name | P 1 |
Unit cell lengths | 76.140, 111.030, 167.260 |
Unit cell angles | 90.03, 101.69, 105.05 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.2162 |
Rwork | 0.213 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4lf1 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.000 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | BUSTER (2.10.0) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 91.970 | 91.970 | 2.050 |
High resolution limit [Å] | 2.000 | 8.940 | 2.000 |
Rmerge | 0.093 | 0.050 | 0.799 |
Rmeas | 0.116 | 0.062 | 1.015 |
Total number of observations | 824839 | ||
Number of reflections | 318354 | 3622 | 21522 |
<I/σ(I)> | 6 | 14.52 | 1.14 |
Completeness [%] | 90.8 | 92 | 82.8 |
Redundancy | 2.6 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | Protein storage buffer: 20 mM Tris, pH 8.0, 300 mM NaCl, 10% Glycerol, 10 mM MgCl2, 20 mM NaHCO3. Reservoir solution: 20-24% PEG 3350, 200 mM sodium sulfate, 100 mM Bis-Tris Propane pH 7.0-8.0. |