1AVP

STRUCTURE OF HUMAN ADENOVIRUS 2 PROTEINASE WITH ITS 11 AMINO ACID COFACTOR

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	300
Detector technology	DIFFRACTOMETER
Collection date	1995-05-10
Detector	ENRAF-NONIUS FAST
Spacegroup name	P 61
Unit cell lengths	114.300, 114.300, 50.000
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	6.000 - 2.600
R-factor	0.184
Rwork	0.184
R-free	0.23300
Structure solution method	SIRAS SOFTWARE USED : NULL STARTING MODEL FOR MOLECULAR REPLACEMENT: NULL
RMSD bond length	0.008
RMSD bond angle	23.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.690
High resolution limit [Å]	2.600	2.600
Rmerge	0.077	0.145
Number of reflections	11559
<I/σ(I)>	20	16
Completeness [%]	98.8	97.6
Redundancy	5	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *		McGrath, W.J., (1996) J. Struct. Biol., 117, 77. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	HEPES	100 (mM)	pH7.5
2	1	reservoir	sodium acetate	1.4-1.6 (M)