4BBO

Crystal structure of core-bradavidin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Collection date	2005-04-21
Spacegroup name	P 21 21 21
Unit cell lengths	49.946, 78.647, 100.120
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	61.900 - 1.600
R-factor	0.14843
Rwork	0.147
R-free	0.17863
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2y32
RMSD bond length	0.012
RMSD bond angle	1.457
Data reduction software	XDS
Phasing software	PHASER
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.700
High resolution limit [Å]	1.600	1.600
Rmerge	0.090	0.550
Number of reflections	52798
<I/σ(I)>	18	4
Completeness [%]	100.0	100
Redundancy	9.6	9.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP			ONE MICROLITER OF THE PROTEIN SOLUTION (LESS THAN 1 MG PER ML AND IN 50 MM SODIUM ACETATE, 100 MM NACL, PH 4) WAS CRYSTALLIZED BY ADDING ONE MICROLITER OF THE WELL SOLUTION (0.1 M HEPES PH 7.4, 0.8 M K,NA TARTRATE).HANGING DROPS AND VAPOUR DIFFUSION METHOD WAS USED AT RT. BEFORE CRYSTALLIZATION, 25 MICROLITERS OF THE PROTEIN SAMPLE WAS INCUBATED WITH 1 MICRO LITER OF BIOTIN SOLUTION (1 MG PER ML AND IN 5 MM TRIS PH 8.8, 8 MM CHES PH 9.5) FOR 3.5 HOURS AT 37 DEGREES OF CELCIUS.