1GD7

CRYSTAL STRUCTURE OF A BIFUNCTIONAL PROTEIN (CSAA) WITH EXPORT-RELATED CHAPERONE AND TRNA-BINDING ACTIVITIES.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44B2
Synchrotron site	SPring-8
Beamline	BL44B2
Temperature [K]	100
Detector technology	CCD
Collection date	1999-06-20
Detector	MAR CCD 165 mm
Spacegroup name	P 43
Unit cell lengths	55.715, 55.715, 167.064
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.000
R-factor	0.217 *
Rwork	0.217
R-free	0.27700
RMSD bond length	0.007
RMSD bond angle	0.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.043	0.191
Total number of observations	135225 *
Number of reflections	33368
<I/σ(I)>	14.7
Completeness [%]	97.5	94.5 *
Redundancy	4	4.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	20 *	NaCl, Sodium Acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	14 (mg/ml)
2	1	reservoir		3.8 (M)
3	1	reservoir	sodium acetate	0.1 (M)