1FQE

CRYSTAL STRUCTURES OF MUTANT (K206A) THAT ABOLISH THE DILYSINE INTERACTION IN THE N-LOBE OF HUMAN TRANSFERRIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	2000-02-11
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	43.900, 57.300, 135.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.730 - 1.800
R-factor	0.196
Rwork	0.196
R-free	0.23700
RMSD bond length	0.008
RMSD bond angle	1.400
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	14.730	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.071	0.185
Total number of observations	373302 *
Number of reflections	29721
<I/σ(I)>	7.4
Completeness [%]	91.2	82.1
Redundancy	3.1	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	293	20-25% PolyEthyleneGlycol 3350, 100mM Potassium acetate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	35 (mg/ml)
2	1	drop	ammonium bicarbonate	0.1 (M)
3	1	reservoir	potassium acetate	0.1 (M)
4	1	reservoir	PEG3350	20-25 (%)