1EFV

THREE-DIMENSIONAL STRUCTURE OF HUMAN ELECTRON TRANSFER FLAVOPROTEIN TO 2.1 A RESOLUTION

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1994-04
Detector	RIGAKU RAXIS II
Spacegroup name	P 1 21 1
Unit cell lengths	47.437, 103.872, 63.696
Unit cell angles	90.00, 109.98, 90.00

Refinement procedure

Resolution	8.000 - 2.100
R-factor	0.171 *
Rwork	0.172
R-free	0.22100 *
Structure solution method	MULTIPLE ISOMORPHOUS REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	24.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASES
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.140
High resolution limit [Å]	2.100	2.100
Rmerge	0.064	0.304 *
Total number of observations	118435 *
Number of reflections	32383
<I/σ(I)>	17	2.6
Completeness [%]	95.6 *	92.4
Redundancy	3.7	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	19 *	THE PROTEIN WAS CRYSTALLIZED FROM 15 % PEG 1500, 50 MM HEPES, PH 7.0. EQUAL VOLUMES OF PROTEIN (15 MG/ML) AND PRECIPITANT WERE MIXED IN SITTING DROPS., vapor diffusion - sitting drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	PEG1500	15 (%)
3	1	drop	HEPES	50 (mM)
4	1	reservoir	PEG1500	15 (%)
5	1	reservoir	HEPES	50 (mM)