4CNW

Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Synchrotron site	Australian Synchrotron
Beamline	MX1
Temperature [K]	100
Detector technology	CCD
Collection date	2012-12-20
Detector	ADSC CCD
Spacegroup name	P 1 21 1
Unit cell lengths	42.167, 134.314, 46.755
Unit cell angles	90.00, 104.04, 90.00

Refinement procedure

Resolution	38.000 - 2.030
R-factor	0.21685
Rwork	0.215
R-free	0.25887
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ml2
RMSD bond length	0.009
RMSD bond angle	1.269
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.7.0032)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.400	2.140
High resolution limit [Å]	2.030	2.030
Rmerge	0.070	0.180
Number of reflections	30083
<I/σ(I)>	22.9	10.8
Completeness [%]	92.4	96.1
Redundancy	7.5	7.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		8		PROTEIN WAS AT 10 MG/ML. THE RESERVOIR CONDITIONS WERE: 25% PEG MME 2000, 200 MM CALCIUM ACETATE, 50 MM TRIS BUFFER PH 8.0. THE CRYSTALS WERE OBTAINED THROUGH CROSS SEEDING FROM A DIFFERENT MUTANT CA-II CRYSTAL.