1L2A

The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-11-19
Detector	MARRESEARCH
Wavelength(s)	0.9340
Spacegroup name	P 21 21 21
Unit cell lengths	148.027, 207.640, 215.354
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.500
R-factor	0.18312
Rwork	0.181
R-free	0.22600 *
RMSD bond length	0.013
RMSD bond angle	1.440 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.054 *	0.245 *
Number of reflections	223075
Completeness [%]	95.2	90.5
Redundancy	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.2 *	291	22% Ammonium sulphate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)	pH7.2
3	1	reservoir	Tris-HCl	100 (mM)	pH7.4
4	1	reservoir	ammonium sulfate	20-22 (%(w/v))