1I4K

CRYSTAL STRUCTURE OF AN SM-LIKE PROTEIN (AF-SM1) FROM ARCHAEOGLOBUS FULGIDUS AT 2.5A RESOLUTION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-04-14
Detector	MARRESEARCH
Wavelength(s)	0.842
Spacegroup name	P 1 21 1
Unit cell lengths	110.397, 64.563, 129.862
Unit cell angles	90.00, 92.09, 90.00

Refinement procedure

Resolution	20.000 - 2.500
R-factor	0.207 *
Rwork	0.207
R-free	0.26400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	A seven membered ring of an Sm-like protein from Pyrococcus abyssii.
RMSD bond length	0.008
RMSD bond angle	1.500
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.072 *	0.353 *
Total number of observations	255898 *
Number of reflections	63291
<I/σ(I)>	14.1	3.5
Completeness [%]	99.3	99.9
Redundancy	4.04	3.34

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.3	20 *	PEG 6000, sodium citrate, pH 4.3, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	11 (mg/ml)
2	1	reservoir	PEG6000	12 (%)
3	1	reservoir	sodium citrate	100 (mM)	pH4.3