4CNX

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	41.591, 67.937, 43.134
Unit cell angles	90.00, 103.07, 90.00

Refinement procedure

Resolution	35.760 - 1.230
R-factor	0.11244
Rwork	0.111
R-free	0.14683
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ml2
RMSD bond length	0.021
RMSD bond angle	2.069
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]	42.000	1.300
High resolution limit [Å]	1.230	1.230
Rmerge	0.040	0.320
Number of reflections	66095
<I/σ(I)>	28.7	6.2
Completeness [%]	98.6	95.2
Redundancy	7.3	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	5.5	281	PROTEIN WAS AT 10 MG/ML. THE RESERVOIR CONDITIONS WERE: 40% PEG 600, 100 MM SODIUM CITRATE AT PH 5.5 SET UP AT 8C. CROSS SEEDING FROM OTHER MUTANT CA-II CRYSTALS WAS USED TO OBTAIN THESE CRYSTALS.