1UGG

HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)-ORTHORHOMBIC FORM

Experimental procedure

Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-01-17
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 21
Unit cell lengths	42.500, 72.700, 75.100
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.500 - 2.200
R-factor	0.179
Rwork	0.179
R-free	0.28200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	CAII A65S-P21 MUTANT (SCOLNICK & CHRISTIAN 1996 IN PRESS)
RMSD bond length	0.010
RMSD bond angle	25.900 *
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]	8.900	2.260
High resolution limit [Å]	2.200	2.200
Rmerge	0.091 *
Total number of observations	27183 *
Number of reflections	11298
<I/σ(I)>	5.9	2.5
Completeness [%]	92.7	88
Redundancy	2.4	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	4.7		50MM TRIS-HCL, PH=8.0, 1.95 - 3.9M NH4SO4, pH 4.7

Crystallization Reagents in Literatures

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