8QMV

L2 forming RubisCO derived from ancestral sequence reconstruction of the last common ancestor of Form I'' and Form I RubisCOs

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Synchrotron site	PETRA III, EMBL c/o DESY
Beamline	P14 (MX2)
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-12-02
Detector	DECTRIS EIGER2 X CdTe 16M
Wavelength(s)	0.6888
Spacegroup name	C 2 2 21
Unit cell lengths	121.790, 203.800, 147.370
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.970 - 1.850
R-factor	0.1609
Rwork	0.161
R-free	0.17390
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	0.666
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX ((1.20.1_4487: ???))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	24.970	24.970	1.900
High resolution limit [Å]	1.850	8.270	1.850
Rmerge	0.113	0.034	1.077
Rmeas	0.117	0.036	1.126
Number of reflections	155284	1829	11329
<I/σ(I)>	16.04
Completeness [%]	99.9
Redundancy	13.9
CC(1/2)	0.999	1.000	0.730

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	289	Purified enzyme (10 mg/mL) in 25 mM Tricine-NaOH, 75 mM NaCl, pH 8.0 was incubated at 3% (v/v) CO2 in air and 30 degrees C for 1 hour in the presence of 0.3 mM CABP and 4.8 mM MgCl2. The enzyme was then mixed in a 1:1 ratio with 0.1 M TRIS pH 8.5, 0.2 M magnesium chloride, 30 % (v/v) polyethylene glycol 400. The crystals were flash frozen in liquid nitrogen.