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.