1E0X

XYLANASE 10A FROM SREPTOMYCES LIVIDANS. XYLOBIOSYL-ENZYME INTERMEDIATE AT 1.65 A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-11-15
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	49.210, 81.060, 72.810
Unit cell angles	90.00, 102.79, 90.00

Refinement procedure

Resolution	15.000 - 1.650
R-factor	0.12 *
Rwork	0.126
R-free	0.16200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	NATIVE STRUCTURE AT 1.2
RMSD bond length	0.012
RMSD bond angle	0.028
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	1.710
High resolution limit [Å]	1.650	1.650
Rmerge	0.033	0.097
Number of reflections	66881
<I/σ(I)>	35.6	12.9
Completeness [%]	99.0	94
Redundancy	3.5	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		PROTEIN WAS CRYSTALLISED WITH 18 % PEG 5000 AS PRECIPITANT, 100MM HEPES PH 7.5 AS BUFFER, 10% ISOPROPANOL, CRYSTAL WERE SOAKED IN PRESENCE OF POWDERED SUBSTRATE FOR 12 HOURS. 15% GLYCEROL WAS ADDED AS CRYOPROTECTANT

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium HEPES	0.1 (M)
2	1	reservoir	PEG5000	18 (%(w/v))
3	1	drop	protein	30 (mg/ml)
4	1	drop	isopropanol	10 (%(v/v))