1UGF

HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)

Experimental procedure

Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-01-15
Detector	RIGAKU
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	0.173
Rwork	0.173
R-free	0.23200
Structure solution method	DIFFERENCE FOURIER
Starting model (for MR)	NATIVE CAII (HAKANSSON ET AL. 1992)
RMSD bond length	0.007
RMSD bond angle	25.200 *
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]	7.200	2.050
High resolution limit [Å]	2.000	2.000
Rmerge	0.059 *	0.160 *
Total number of observations	41320 *
Number of reflections	17315
<I/σ(I)>	8	3.2
Completeness [%]	94.7	74.6
Redundancy	2	2.4

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	drop	methylmercury acetate
3	1	reservoir	ammonium sulfate	1.95-3.9 (M)