1NJU

Complex structure of HCMV Protease and a peptidomimetic inhibitor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	CCD
Collection date	2001-07-06
Detector	ADSC QUANTUM 4
Wavelength(s)	1.00000
Spacegroup name	P 21 21 2
Unit cell lengths	105.460, 213.530, 52.330
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 2.700
R-factor	0.223
Rwork	0.223
R-free	0.27100 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	23.100 *
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]	30.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.070 *
Total number of observations	143394 *
Number of reflections	32973
Completeness [%]	95.2	93.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	21 *	PEG 4000, HEPES, EDTA, Sodium Chloride, Sodium Sulfate, DTT, Spermine_HCl, Glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7 (mg/ml)
10	1	reservoir	glycerol	10-12 (%)
11	1	reservoir		0.3 (M)
12	1	reservoir	spermine-HCl	5 (mM)
13	1	reservoir	dithiothreitol	2 (mM)
14	1	reservoir	EDTA	2 (mM)
2	1	drop	HEPES	20 (mM)	pH7.0
3	1	drop		80 (mM)
4	1	drop		40 (mM)
5	1	drop	dithiothreitol	2 (mM)
6	1	drop	EDTA	2 (mM)
7	1	drop	DMF	2 (mM)
8	1	reservoir	PEG4000	16-18 (%)
9	1	reservoir	HEPES	0.1 (M)	pH7.0