1NJT

COMPLEX STRUCTURE OF HCMV PROTEASE AND A PEPTIDOMIMETIC INHIBITOR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	CCD
Collection date	2001-08-13
Detector	CUSTOM-MADE
Wavelength(s)	0.97970
Spacegroup name	P 21 21 2
Unit cell lengths	107.072, 213.306, 52.795
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 2.500
R-factor	0.228
Rwork	0.228
R-free	0.27300 *
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]	50.000	2.630
High resolution limit [Å]	2.500	2.500
Rmerge	0.060 *
Total number of observations	182204 *
Number of reflections	43637
Completeness [%]	85.0	72.7

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