1HUS

RIBOSOMAL PROTEIN S7

Experimental procedure

Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	293
Detector technology	CCD
Collection date	1997-03
Detector	PRINCETON 2K
Spacegroup name	P 21 21 2
Unit cell lengths	54.400, 131.020, 29.150
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.500
R-factor	0.216
Rwork	0.216
R-free	0.27000
Structure solution method	MAD WITH SE-MET MUTANT
RMSD bond length	0.020
RMSD bond angle	25.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.540
High resolution limit [Å]	2.500	2.500
Rmerge	0.048	0.138
Total number of observations	53236 *
Number of reflections	7586
<I/σ(I)>	20.3	5.8
Completeness [%]	97.6	92.9
Redundancy	2.8	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	8.2		PROTEIN WAS CRYSTALLIZED FROM 0.1M NA HEPES BUFFER(PH8.2) WITH 4%(V/V) 2-PROPANOL AND 2.0M AMMONIUM SULFATE.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	sodium HEPES	0.1 (M)
2	1	1	2-propanol	4 (%(v/v))
3	1	1	ammonium sulfate	2.0 (M)