1HT3

MERCURY INDUCED MODIFICATIONS IN THE STEREOCHEMISTRY OF THE ACTIVE SITE THROUGH CYS-73 IN A SERINE PROTEASE: CRYSTAL STRUCTURE OF THE COMPLEX OF A PARTIALLY MODIFIED PROTEINASE K WITH MERCURY AT 1.8 A RESOLUTION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	277
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	P 43 21 2
Unit cell lengths	68.360, 68.360, 108.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.800
R-factor	0.164
Rwork	0.164
R-free	0.22100
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.012
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.053	0.165
Number of reflections	21939
<I/σ(I)>	10.1	4.3
Completeness [%]	98.3	98
Redundancy	6.2	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	277	sodium nitrate, calcium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K