1GGV

CRYSTAL STRUCTURE OF THE C123S MUTANT OF DIENELACTONE HYDROLASE (DLH) BOUND WITH THE PMS MOIETY OF THE PROTEASE INHIBITOR, PHENYLMETHYLSULFONYL FLUORIDE (PMSF)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1994-12-08
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 21 21 21
Unit cell lengths	51.080, 51.860, 82.610
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	7.000 - 2.500
R-factor	0.151
Rwork	0.151
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	DIENELACTONE HYDROLASE (WILD-TYPE)
RMSD bond length	0.010
RMSD bond angle	24.240 *
Data reduction software	MANUFACTURER (SUPPLIED (MSC))
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.090
High resolution limit [Å]	2.000	2.000
Rmerge	0.117 *
Total number of observations	30250 *
Number of reflections	12109
Completeness [%]	78.7	65.2
Redundancy	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.3	291	(K+/Na+) phosphate, PMSF, pH 6.3, vapor diffusion/hanging drop, temperature 291.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	phosphate	3 (M)
3	1	reservoir	phosphate	1.6-1.8 (M)
4	1	drop	PMSF	50-100 (mM)	in 2-propanol