5HJX

Structure function studies of R. palustris RubisCO (A47V 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	2014-03-01
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.9797
Spacegroup name	P 1
Unit cell lengths	75.960, 100.250, 100.380
Unit cell angles	113.06, 108.07, 88.89

Refinement procedure

Resolution	87.220 - 1.799
R-factor	0.1855
Rwork	0.183
R-free	0.20930
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4lf1
RMSD bond length	0.005
RMSD bond angle	0.827
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	87.220	87.220	1.850
High resolution limit [Å]	1.799	8.050	1.799
Rmerge	0.055	0.042	0.385
Rmeas	0.078	0.059	0.544
Total number of observations	388868
Number of reflections	208202	2281	15537
<I/σ(I)>	7.98	17.74	1.9
Completeness [%]	87.0	84.4	87.6
Redundancy	1.9		1.8

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