1HEK

Crystal structure of equine infectious anaemia virus matrix antigen (EIAV MA)

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-04-15
Detector	MARRESEARCH
Wavelength(s)	0.9116, 0.9781, 0.9778
Spacegroup name	P 65
Unit cell lengths	47.150, 47.150, 204.770
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	23.780 - 2.800
R-factor	0.279
Rwork	0.279
R-free	0.37300
Structure solution method	MAD
RMSD bond length	0.015
RMSD bond angle	21.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.000	2.900
High resolution limit [Å]	2.800	2.800
Rmerge	0.074	0.600
Total number of observations	19170 *
Number of reflections	6347	633 *
<I/σ(I)>	11.4
Completeness [%]	99.0	99
Redundancy	3	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	6.5	18 *	30% PEG5000, 0.2M AMMONIUM SULFATE, 0.1M MES (PH6.5), 291K, pH 6.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG5000	30 (%(w/v))
2	1	reservoir	ammonium sulfate	0.2 (M)
3	1	reservoir	MES	0.1 (M)	pH6.5
4	1	drop	protein	2.5 (mg/ml)