1EEJ

CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE, DSBC, FROM ESCHERICHIA COLI

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-10-29
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	59.336, 78.149, 94.489
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.210 - 1.900
R-factor	0.214
Rwork	0.214
R-free	0.24700
RMSD bond length	0.005
RMSD bond angle	23.300 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.048	0.322
Number of reflections	35436
<I/σ(I)>	24.6
Completeness [%]	99.5	99.5
Redundancy	4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5 *	291	PEG 550 (MME), MES , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	30 (mg/ml)
2	1	reservoir	PEG4000	25 (%)
3	1	reservoir	isopropanol	50 (%)