1US2

Xylanase10C (mutant E385A) from Cellvibrio japonicus in complex with xylopentaose

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	100
Detector technology	CCD
Collection date	2001-05-15
Detector	ADSC QUANTUM 4
Spacegroup name	P 21 21 21
Unit cell lengths	44.597, 82.686, 170.727
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 1.850
R-factor	0.181
Rwork	0.179
R-free	0.23000 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1clx
RMSD bond length	0.017
RMSD bond angle	1.400 *
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]	20.000	1.920
High resolution limit [Å]	1.850	1.850
Rmerge	0.080	0.370
Number of reflections	53227
<I/σ(I)>	18.5	4.8
Completeness [%]	98.0	98
Redundancy	4.4	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7	18 *	30 MG/ML PROTEIN 0.2 M SODIUM IODIDE, 20% PEG 3350, 20 MM (1 UL) XYLOPENTAOSE, pH 7.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	30 (mg/ml)
2	1	reservoir	sodium iodide	0.2 (M)
3	1	reservoir	PEG3350	20 (%(w/v))
4	1	reservoir	xylopentaose	20 (mM)