5HK4

Structure function studies of R. palustris RubisCO (A47V-M331A mutant)

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	2014-03-01
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.9797
Spacegroup name	P 1
Unit cell lengths	76.090, 100.410, 100.320
Unit cell angles	113.06, 88.86, 108.01

Refinement procedure

Resolution	81.960 - 2.150
R-factor	0.228
Rwork	0.225
R-free	0.25500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4lf1
RMSD bond length	0.004
RMSD bond angle	0.756
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]	81.960	2.210
High resolution limit [Å]	2.150	2.150
Rmerge	0.115	0.329
Number of reflections	133906
<I/σ(I)>	11.88	1.9
Completeness [%]	95.2	87.6
Redundancy	4.3	1.75

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. Protein concentration: 16 mg/ml. Reservoir solution: 20-24% PEG 3350, 200 mM sodium sulfate, 100 mM Bis-Tris Propane pH 7-8.