1VSK

ASV INTEGRASE CORE DOMAIN D64N MUTATION IN CITRATE BUFFER PH 6.0

Experimental procedure

Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR591
Temperature [K]	295
Detector technology	IMAGE PLATE
Collection date	1997-10-31
Detector	MAC Science DIP-2000
Spacegroup name	P 43 21 2
Unit cell lengths	67.159, 67.159, 79.651
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.200
R-factor	0.159
Rwork	0.159
R-free	0.24900
Starting model (for MR)	1asv
RMSD bond length	0.014
RMSD bond angle	25.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.210
High resolution limit [Å]	2.150	2.150
Rmerge	0.077 *	0.415 *
Total number of observations	85055 *
Number of reflections	10132
<I/σ(I)>	20.7	3.6
Completeness [%]	97.0	96.5
Redundancy	8.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *		Bujacz, G., (1995) J. Mol. Biol., 253, 333. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6-7.5 (mg/ml)
2	1	reservoir	HEPES	100 (mM)
3	1	reservoir	isopropanol	10 (%)
4	1	reservoir	PEG4000	20 (%)