1QB2

CRYSTAL STRUCTURE OF THE CONSERVED SUBDOMAIN OF HUMAN PROTEIN SRP54M AT 2.1A RESOLUTION: EVIDENCE FOR THE MECHANISM OF SIGNAL PEPTIDE BINDING

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	CCD
Collection date	1998-09-13
Detector	BRANDEIS
Spacegroup name	P 21 21 21
Unit cell lengths	28.910, 61.340, 129.220
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.100
Rwork	0.245
R-free	0.31800
RMSD bond length	0.008
RMSD bond angle	1.065
Data reduction software	MADNESS
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.140
High resolution limit [Å]	2.100	2.100
Rmerge	0.057	0.296
Total number of observations	165944 *
Number of reflections	25000
Completeness [%]	99.0	94
Redundancy	3.5	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	4.6	4 *	30% PEG 2K, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
1	Vapor diffusion, sitting drop *	4.6	4 *	30% PEG 2K, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
1	Vapor diffusion, sitting drop *	4.6	4 *	30% PEG 2K, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
1	Vapor diffusion, sitting drop *	4.6	4 *	30% PEG 2K, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	25 (mg/ml)
2	1	drop		0.15 (M)
3	1	drop	Tris-HCl	50 (mM)	pH8.0
4	1	drop	PEG2000 MME	25 (%(w/v))
5	1	drop	ammonium sulfate	0.2 (M)
6	1	drop	sodium acetate	0.1 (M)	pH4.6
7	1	reservoir	glycerol	15 (%(v/v))