3GZ0

Apo-human carbonic anhydrase II revisited: Implications of the loss of a metal in protein structure, stability and solvent network

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE A1
Synchrotron site	CHESS
Beamline	A1
Temperature [K]	100
Detector technology	CCD
Collection date	2007-10-01
Detector	ADSC QUANTUM 210
Spacegroup name	P 1 21 1
Unit cell lengths	42.737, 41.623, 72.821
Unit cell angles	90.00, 104.59, 90.00

Refinement procedure

Resolution	50.000 - 1.260
R-factor	0.14
Rwork	0.140
R-free	0.18700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2cba
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000
High resolution limit [Å]	1.260	1.260
Number of reflections	91749
Completeness [%]	93.4	93.4
Redundancy	7.1	7.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	rystals of apo-HCA II were obtained through hanging drop method. 10 ul drops of equal amounts of protein and precipitant were equilibrated against precipitant solution (1.3 M Sodium Citrate, 100mM Tris-HCl, pH 7.0) by vapor diffusion at room temperature (~20 C). A crystal was cryoprotected by quick immersion into 20% glycerol mother liquor and flash-cooled by exposing it to a gas stream of nitrogen at 100K, vapor diffusion, hanging drop, temperature 293K