4CNV

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	41.757, 69.276, 44.578
Unit cell angles	90.00, 107.76, 90.00

Refinement procedure

Resolution	34.660 - 1.620
R-factor	0.1449
Rwork	0.143
R-free	0.18219
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ml2
RMSD bond length	0.023
RMSD bond angle	2.104
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]	42.500	1.700
High resolution limit [Å]	1.620	1.620
Rmerge	0.110	0.640
Number of reflections	30981
<I/σ(I)>	16.3	3.2
Completeness [%]	99.9	99.5
Redundancy	7.4	7.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		6		PROTEIN WAS AT 10 MG/ML; THE RESERVOIR SOLUTION WAS 5% PEG 1000, 30% PEG 600, 10% GLYCEROL, 100 MM SODIUM MES BUFFER AT PH 6. SEEDS OF THE MUT1 FORM WERE USED TO OBTAIN THESE CRYSTALS.