5HQL

Structure function studies of R. palustris RubisCO (A47V-M331A mutant; CABP-bound; no expression tag)

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	2014-11-26
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.9792
Spacegroup name	P 1
Unit cell lengths	74.443, 100.491, 103.965
Unit cell angles	108.13, 113.66, 95.44

Refinement procedure

Resolution	87.961 - 2.530
R-factor	0.2179
Rwork	0.213
R-free	0.25850
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4lf1
RMSD bond length	0.005
RMSD bond angle	1.038
Data reduction software	XDS
Data scaling software	Aimless (0.1.27)
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	87.961	92.340	2.660
High resolution limit [Å]	2.530	7.990	2.530
Rmerge	0.170	0.094	0.697
Rpim	0.116	0.060	0.536
Total number of observations	214324	8392	26186
Number of reflections	77023
<I/σ(I)>	4.3	11.5	1.2
Completeness [%]	90.1	89.2	88.3
Redundancy	2.8	3.5	2.4
CC(1/2)	0.972	0.974	0.634

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		291	Reservoir solution: 20-24% PEG 3350, 200 mM sodium sulfate, 100 mM Bis-Tris Propane pH 7.0-8.0. Protein storage buffer: 20 mM Tris, pH 8.0, 300 mM NaCl, 10% Glycerol, 10 mM MgCl2, 20 mM NaHCO3.