1OCB

Structure of the wild-type cellobiohydrolase Cel6A from Humicolas insolens in complex with a fluorescent substrate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2000-11-15
Detector	ADSC CCD
Spacegroup name	P 1 21 1
Unit cell lengths	49.763, 155.681, 51.218
Unit cell angles	90.00, 118.42, 90.00

Refinement procedure

Resolution	40.000 * - 1.750
R-factor	0.135
Rwork	0.133
R-free	0.17200 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2bvw
RMSD bond length	0.017 *
RMSD bond angle	1.620 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	1.810
High resolution limit [Å]	1.750	1.750
Rmerge	0.041	0.128
Number of reflections	69418
<I/σ(I)>	17.3	6
Completeness [%]	97.5	91.3
Redundancy	2.2	2.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7 *		THE PROTEIN WAS CONCENTRATED IN WATER TO 7 MG/ML IT WAS INCUBATED 1H PRIOR CRYSTALLISATION WITH THE 5MM OF THE SUBSTRATE 16% PEG5KMME AND 200 MM CALCIUM ACETATE WERE USED AS PRECIPITANT AND 100 MM SODIUM ACETATE PH 4.6 AS BUFFER.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	HEPES	100 (mM)	pH7.0
2	1	reservoir	calcium acetate	200 (mM)
3	1	reservoir	PEG8000	18 (%)