2FMG

Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine and crystallographic analysis of their adducts with isozyme II: sterospecific recognition within the active site of an enzyme and its consequences for the drug design, structure with L-phenylalanine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SEALED TUBE
Source details	OXFORD DIFFRACTION ENHANCE ULTRA
Temperature [K]	100
Detector technology	CCD
Collection date	2005-10-27
Detector	OXFORD SAPPHIRE CCD
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	41.990, 41.410, 72.200
Unit cell angles	90.00, 104.40, 90.00

Refinement procedure

Resolution	15.000 - 1.600
Rwork	0.220
R-free	0.24000
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	1.360
Data reduction software	MOSFLM
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.680
High resolution limit [Å]	1.600	1.600
Rmerge	0.095
Number of reflections	29735
<I/σ(I)>	11.3
Completeness [%]	34.0	40

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.7	277	2.4-2.5 M (NH4)2SO4 in 50mM Tris.HCl pH 7.7-7.8, 1 mM sodium 4-(hydroxymercury)benzoate, VAPOR DIFFUSION, HANGING DROP, temperature 277K