1IS9

Endoglucanase A from Clostridium thermocellum at atomic resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-08-01
Detector	MARRESEARCH
Wavelength(s)	0.801, 1.008, 1.006
Spacegroup name	P 21 21 21
Unit cell lengths	49.441, 62.829, 103.891
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 - 1.030
Rwork	0.131
R-free	0.14900
Structure solution method	MAD
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	1.030
High resolution limit [Å]	1.030 *	1.020
Rmerge	0.049 *	0.355 *
Total number of observations	1605139 *
Number of reflections	158384
<I/σ(I)>	14	3
Completeness [%]	98.2 *	90.9 *
Redundancy	4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7.5 *		macroseeding, Souchon, H., (1996) Proteins: Struct.,Funct., Genet., 25, 134. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	Tris	0.1 (M)	pH7.5
2	1	1		0.2 (M)
3	1	1	PEG4000	17 (%)
4	1	2	Tris-HCl	0.1 (M)	pH7.2
5	1	2	PEG8000	15 (%)