261L

STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE A1
Synchrotron site	CHESS
Beamline	A1
Temperature [K]	298
Detector technology	CCD
Detector	ADSC QUANTUM 1
Spacegroup name	P 32 2 1
Unit cell lengths	61.125, 61.125, 97.338
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.500
R-factor	0.17 *
Rwork	0.170
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	CYS-FREE VERSION OF T4-LYSOZYME
RMSD bond length	0.010
RMSD bond angle	0.000 *
Data reduction software	MOSFLM
Data scaling software	XDS ((SCALA))
Phasing software	TNT
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000
High resolution limit [Å]	2.500	2.500
Rmerge	0.084	0.200
Number of reflections	28161
<I/σ(I)>		2
Completeness [%]	86.5
Redundancy	4.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7.5		CRYSTALS WERE GROWN FROM 20% POLYETHYLENE GLYCOL 6000, 20% ISOPROPANOL, 50MM TRIS-HCL PH 7.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	20 (mg/ml)
2	1	1	PEG6000	20 (%)
3	1	1	isopropanol	20 (%)
4	1	1	Tris-HCl	50 (mM)