1AIH

CATALYTIC DOMAIN OF BACTERIOPHAGE HP1 INTEGRASE

Experimental procedure

Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F2
Synchrotron site	CHESS
Beamline	F2
Temperature [K]	95
Detector technology	CCD
Collection date	1996-12-12
Detector	PRINCETON 2K
Spacegroup name	P 21 21 21
Unit cell lengths	42.400, 129.300, 234.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.500
R-factor	0.209
Rwork	0.209
R-free	0.27200
Structure solution method	MAD
RMSD bond length	0.008
RMSD bond angle	22.480 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASES
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.780
High resolution limit [Å]	2.700	2.700
Rmerge	0.087	0.180
Total number of observations	52126 *
Number of reflections	34819
<I/σ(I)>	11.4	5
Completeness [%]	97.0	89.7
Redundancy	6	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5 *		VAPOR DIFFUSION, 15% PEG 8000, 45MM NA CAODYLATE, 34MM AMMONIUM SULFATE, 10MM TRIS-HCL, 4.5% GLYCEROL, 0.1 M MGCL., pH 7.5, vapor diffusion

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	9 (mg/ml)
2	1	reservoir	PEG8000	15-17 (%)
3	1	reservoir	magnesium acetate	0.2 (M)
4	1	reservoir	sodium cacodylate	0.1 (M)
5	1	drop	ammonium sulfate