1MEP

Crystal Structure of Streptavidin Double Mutant S45A/D128A with Biotin: Cooperative Hydrogen-Bond Interactions in the Streptavidin-Biotin System.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-1
Synchrotron site	SSRL
Beamline	BL9-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-04-01
Detector	MARRESEARCH
Wavelength(s)	0.97
Spacegroup name	P 1 21 1
Unit cell lengths	50.645, 97.857, 52.168
Unit cell angles	90.00, 112.28, 90.00

Refinement procedure

Resolution	10.000 - 1.650
R-factor	0.204
Rwork	0.201
R-free	0.29500 *
Structure solution method	ISOMORPHOUS
Starting model (for MR)	1swe
RMSD bond length	0.007
RMSD bond angle	0.027
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELX
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.680
High resolution limit [Å]	1.650	1.650
Rmerge	0.099	0.542
Total number of observations	1009902 *
Number of reflections	57334
<I/σ(I)>	14.8	1.5
Completeness [%]	99.6	98.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	294	sodium citrate, cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	sodium citrate	1.0 (M)
3	1	reservoir	cacodylate	0.1 (M)	pH6.5