1E0V

Xylanase 10A from Sreptomyces lividans. cellobiosyl-enzyme intermediate at 1.7 A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-09-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	67.870, 46.270, 87.070
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 1.700
R-factor	0.15 *
Rwork	0.158
R-free	0.19900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	NATIVE STRUCTURE AT 1.2
RMSD bond length	0.007
RMSD bond angle	0.022
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.032	0.121
Number of reflections	29439
<I/σ(I)>	36.5	9.4
Completeness [%]	97.0	82
Redundancy	4.3	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		PROTEIN WAS CRYSTALLISED WITH 16 % PEG 4000 AS PRECIPITANT,100MM HEPES PH 7.5 AS BUFFER, 10% ISOPROPANOL, CRYSTAL WERE SOAKED IN PRESENCE OF POWDERED SUBSTR

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium HEPES	0.1 (M)
2	1	reservoir	PEG4000	16 (%(w/v))
3	1	drop	isopropanol	10 (%(v/v))
4	1	drop	protein	30 (mg/ml)