1I1X

1.11 A ATOMIC 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]	293
Detector technology	CCD
Collection date	1999-02-28
Detector	ADSC QUANTUM 4
Wavelength(s)	1.009
Spacegroup name	P 1 21 1
Unit cell lengths	41.520, 68.090, 51.440
Unit cell angles	90.00, 113.56, 90.00

Refinement procedure

Resolution	10.000 - 1.110
Rwork	0.099
R-free	0.12360
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1TUX (1.8 A)
RMSD bond length	0.016
RMSD bond angle	2.100 *
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]	25.000	1.150
High resolution limit [Å]	1.110	1.110
Rmerge	0.052	0.360
Total number of observations	294946 *
Number of reflections	90855
<I/σ(I)>	20.6	3
Completeness [%]	87.5	81.3
Redundancy	3.25 *

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 (%)