5HAO

Structure function studies of R. palustris RubisCO (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	2014-03-01
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.9797
Spacegroup name	P 1
Unit cell lengths	75.750, 100.120, 100.310
Unit cell angles	112.82, 108.14, 88.76

Refinement procedure

Resolution	91.687 - 2.182
R-factor	0.2046
Rwork	0.201
R-free	0.23260
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4lf1
RMSD bond length	0.015
RMSD bond angle	0.747
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]	91.690	91.690	2.240
High resolution limit [Å]	2.180	9.760	2.180
Rmerge	0.119	0.054	0.523
Rmeas	0.140	0.063	0.616
Total number of observations	441346
Number of reflections	122307	1488	6757
<I/σ(I)>	8.34	21.34	2.27
Completeness [%]	91.5	98.7	68.1
Redundancy	3.6		3.4

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.