1JQ6

HUMAN CYTOMEGALOVIRUS PROTEASE DIMER-INTERFACE MUTANT, S225Y

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-11-09
Detector	FUJI
Wavelength(s)	0.976
Spacegroup name	C 2 2 21
Unit cell lengths	42.270, 108.300, 108.500
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.300 - 2.300
R-factor	0.229 *
Rwork	0.229
R-free	0.28600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1WPO (monomer)
RMSD bond length	0.006
RMSD bond angle	1.200
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	COMO
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.300	2.440
High resolution limit [Å]	2.300	2.300
Rmerge	0.057 *	0.172 *
Total number of observations	38153 *
Number of reflections	10420
Completeness [%]	91.0	93

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5 *	21 *	PEG 8000, sodium cacodylate, magnesium acetate, glycerol, spermine tetrahydrochloride, DTT, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 294K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG8000	16 (%(w/v))
10	1	drop	dithiothreitol	1 (mM)
2	1	reservoir	sodium cacodylate	0.1 (M)
3	1	reservoir		0.15 (M)
4	1	reservoir	glycerol	2.5 (%(v/v))
5	1	reservoir	spermine tetrahydrochloride	20 (mM)
6	1	reservoir	dithiothreitol	2 (mM)
7	1	drop	protein	25 (mg/ml)
8	1	drop		20 (mM)
9	1	drop	EDTA	0.1 (mM)