1FSR

X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	130
Detector technology	IMAGE PLATE
Collection date	2000-01-06
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 1
Unit cell lengths	42.300, 43.800, 67.600
Unit cell angles	86.70, 90.00, 75.60

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.24
Rwork	0.240
R-free	0.29700
RMSD bond length	0.008
RMSD bond angle	1.500
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.085	0.371
Total number of observations	31715 *
Number of reflections	22676
<I/σ(I)>	4.2
Completeness [%]	71.5	60.1
Redundancy	1.4	1.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	25 *	HEPES, PEG 1500, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	HEPES	100 (mM)
3	1	reservoir	PEG1500	25 (%)