1I1W

0.89A Ultra high resolution structure of a Thermostable Xylanase from Thermoascus Aurantiacus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X9B
Synchrotron site	NSLS
Beamline	X9B
Temperature [K]	100
Detector technology	CCD
Collection date	1999-04-03
Detector	ADSC QUANTUM 4
Wavelength(s)	0.98
Spacegroup name	P 1 21 1
Unit cell lengths	41.050, 66.990, 50.760
Unit cell angles	90.00, 113.50, 90.00

Refinement procedure

Resolution	10.000 - 0.890
Rwork	0.090
R-free	0.10610
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	LOCALLY AVAILABLE INTERMEDIATE REFINED ROOM TEMP. 1.11 A MODEL
RMSD bond length	0.036 *
RMSD bond angle	2.540 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000	0.920
High resolution limit [Å]	0.890	0.890
Rmerge	0.047	0.180
Total number of observations	858643 *
Number of reflections	177476
<I/σ(I)>	32.65	7.82
Completeness [%]	92.0	83
Redundancy	4.80 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.2	293	Viswamitra, M.A., (1993) J.Mol.Biol., 232, 987. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	1 (%)
2	1	drop	PEG6000	10 (%(w/v))
3	1	reservoir	PEG6000	50 (%)