1UGA

HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY PHE (A65F)

Experimental procedure

Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995-04-01
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	0.154
Rwork	0.154
R-free	0.24600
Structure solution method	DIFFERENCE FOURIER
Starting model (for MR)	NATIVE CAII HAKANSSON ET AL. 1992
RMSD bond length	0.009
RMSD bond angle	25.300 *
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]	6.500	2.360
High resolution limit [Å]	2.300	2.300
Rmerge	0.103 *
Total number of observations	20445 *
Number of reflections	10085
<I/σ(I)>	6.53	2
Completeness [%]	88.1	89.7
Redundancy	2	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8		pH 8.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris-HCl	50 (mM)
2	1	drop	ammonium sulfate	1.95-3.9 (M)
3	1	reservoir	Tris-HCl	50 (mM)
4	1	reservoir	ammonium sulfate	1.95-3.9 (M)
5	1	drop	enzyme
6	1	drop	dithiothreitol	2 (mM)