2Y32

Crystal structure of bradavidin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-2
Synchrotron site	MAX II
Beamline	I911-2
Temperature [K]	100
Detector technology	CCD
Collection date	2006-06-07
Detector	MARRESEARCH SX-165
Spacegroup name	P 21 21 21
Unit cell lengths	46.712, 84.868, 120.260
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.640 - 1.780
R-factor	0.14639
Rwork	0.144
R-free	0.18243
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	AN ENSEMBLE OF THREE HOMOLOGY MODELS OF BRADAVIDIN BASED ON PDB ENTRIES 1AVD 1mk5 AND 2UYW.
RMSD bond length	0.014
RMSD bond angle	1.382
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.880
High resolution limit [Å]	1.780	1.780
Rmerge	0.090	0.420
Number of reflections	46670
<I/σ(I)>	18	5.9
Completeness [%]	100.0	100
Redundancy	9.6	9.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP			0.7 MICROLITER OF WELL SOLUTION CONTAINING 25% PEG 4000, 0.17 M AMMONIUM ACETATE, AND 0.08 M SODIUM ACETATE, PH 4.6 WERE MIXED WITH 0.8 MICROLITER OF PROTEIN SOLUTION CONTAINING 0.4 MG PER ML OF PROTEIN, 50 MM SODIUM ACETATE, PH 4. THE PROTEIN SOLUTION WAS DILUTED WITH SATURATED SOLUTION OF 4-HYDROXYAZOBENZENE-2-CARBOXYLIC ACID IN 1 TO 10 VOLUME RATIO BEFORE CRYSTALLIZATION, WHICH WAS AT RT USING THE VAPOUR DIFFUSION METHOD AND SITTING DROPS.