1L1Y

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	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-09-30
Detector	MARRESEARCH
Wavelength(s)	0.84410
Spacegroup name	P 21 21 21
Unit cell lengths	147.243, 207.204, 213.220
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.400
R-factor	0.19077
Rwork	0.189
R-free	0.22400 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.330 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.440
High resolution limit [Å]	2.400	2.400
Rmerge	0.077	0.399 *
Number of reflections	254279
Completeness [%]	99.9	100
Redundancy	8.1

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))