1P7N

Dimeric Rous Sarcoma virus Capsid protein structure with an upstream 25-amino acid residue extension of C-terminal of Gag p10 protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-ID-B
Synchrotron site	APS
Beamline	14-ID-B
Temperature [K]	298
Detector technology	CCD
Collection date	2002-06-20
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9
Spacegroup name	P 41 21 2
Unit cell lengths	47.870, 47.870, 170.390
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.500 - 2.600
R-factor	0.26
Rwork	0.260
R-free	0.29800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1em9
RMSD bond length	0.110 *
RMSD bond angle	2.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.540
High resolution limit [Å]	2.450	2.450
Rmerge	0.055	0.329
Number of reflections	6743
Completeness [%]	85.2	51.4
Redundancy	3.18 *	1.4 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8 *	20 *	10 mM HEPES-sodium buffer and 0.8M potassium sodium tartrate tetrahydrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)	pH8.0
3	1	drop		25 (mM)
4	1	reservoir	sodium HEPES	0.1 (M)	pH7.5
5	1	reservoir	potassium sodium tartrate tetrahydrate	0.8 (M)