4BCS

Crystal structure of an avidin mutant

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2011-02-25
Detector	ADSC QUANTUM 210
Spacegroup name	P 21 21 2
Unit cell lengths	81.110, 47.170, 60.610
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.600 - 1.800
R-factor	0.19105
Rwork	0.189
R-free	0.22598
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1wbi
RMSD bond length	0.014
RMSD bond angle	1.870
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.040	0.410
Number of reflections	22157
<I/σ(I)>	30	5
Completeness [%]	100.0	100
Redundancy	7.2	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION			300 NL OF PROTEIN SOLUTION (7.36 MG PER ML; 50 MM SODIUM ACETATE, PH 4) WERE MIXED WITH 300 NL OF WELL SOLUTION (0.09 M PHOSPHATE, CITRATE, PH 4.2; 36% PEG 300). VAPOUR DIFFUSION WAS USED. BEFORE CRYSTALLIZATION, BIOTIN SOLUTION (1 MG PER ML; 5 MM TRIS, PH 8.8 AND 8 MM CHES, PH 9.5) WAS ADDED TO THE PROTEIN SOLUTION IN 1 TO 10 (VOLUME PER VOLUME) RATIO, RESPECTIVELY.