4KGR

Backbone Modifications in the Protein GB1 Helix: beta-3-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 SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2012-04-12
Detector	RIGAKU SATURN 944
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	52.162, 81.168, 52.063
Unit cell angles	90.00, 89.97, 90.00

Refinement procedure

Resolution	32.031 - 2.000
R-factor	0.1619
Rwork	0.158
R-free	0.19200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB 2QMT
RMSD bond length	0.011
RMSD bond angle	1.544
Data reduction software	CrystalClear
Data scaling software	CrystalClear
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.7.3_928))

Data quality characteristics

	Overall
Low resolution limit [Å]	32.031
High resolution limit [Å]	2.000
Rmerge	0.044
Number of reflections	27508
<I/σ(I)>	23.6
Completeness [%]	93.7
Redundancy	3.55

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	298	0.15 M sodium acetate pH 4.6, 20% w/v PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 298K