1UGC

HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY HIS (A65H)

Experimental procedure

Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995-08-10
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 1 21 1
Unit cell lengths	42.700, 41.700, 73.000
Unit cell angles	90.00, 104.60, 90.00

Refinement procedure

Resolution	6.500 - 2.000
R-factor	0.162
Rwork	0.162
R-free	0.22500
Structure solution method	DIFFERENCE FOURIER
Starting model (for MR)	NATIVE CAII (HAKANSSON ET AL. 1992)
RMSD bond length	0.008
RMSD bond angle	25.500 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((AGROVATA)
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	6.700	2.050
High resolution limit [Å]	2.000	2.000
Rmerge	0.048 *	0.148 *
Total number of observations	51671 *
Number of reflections	15547
<I/σ(I)>	12.4	5.1
Completeness [%]	92.5	61.7
Redundancy	3.3	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8		50MM TRIS-HCL, PH=8.0, 1.95 - 3.9M NH4SO4

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris-HCl	50 (mM)
2	1	reservoir	ammonium sulfate	1.95-3.9 (M)
3	1	drop	methylmercury acetate