5HFY

Backbone Modifications in the Protein GB1 Helix: beta-2-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E DW
Temperature [K]	100
Detector technology	CCD
Collection date	2014-06-03
Detector	RIGAKU SATURN 944
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	92.816, 22.415, 65.261
Unit cell angles	90.00, 134.09, 90.00

Refinement procedure

Resolution	23.435 - 1.950
R-factor	0.199
Rwork	0.195
R-free	0.23020
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2qmt
RMSD bond length	0.005
RMSD bond angle	1.043
Data reduction software	d*TREK
Data scaling software	d*TREK
Phasing software	PHENIX
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.440	2.020
High resolution limit [Å]	1.950	1.950
Rmerge	0.069	0.152
Number of reflections	7188
<I/σ(I)>	18.5	3.6
Completeness [%]	97.8	90.4
Redundancy	4.8	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	298	0.2 M sodium acetate pH 4.6, 20% w/v PEG 4000