262L

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	rotating-anode X-ray tube
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	IMAGE PLATE
Spacegroup name	P 1 21 1
Unit cell lengths	57.720, 55.790, 65.180
Unit cell angles	90.00, 110.97, 90.00

Refinement procedure

Resolution	55.000 - 2.500
R-factor	0.227 *
Rwork	0.227
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	CYS-FREE VERSION OF T4-LYSOZYME
RMSD bond length	0.011
RMSD bond angle	18.400 *
Data reduction software	XDS
Data scaling software	XDS
Phasing software	TNT
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	55.000
High resolution limit [Å]	2.500	2.500
Rmerge	0.070 *	0.200
Number of reflections	47089
<I/σ(I)>		2
Completeness [%]	91.0 *
Redundancy	3.5

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)