1FQF

CRYSTAL STRUCTURES OF MUTANT (K296A) THAT ABOLISH THE DILYSINE INTERACTION IN THE N-LOBE OF HUMAN TRANSFERRIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	2000-02-17
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	44.000, 57.000, 132.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.100
R-factor	0.212
Rwork	0.212
R-free	0.29500
RMSD bond length	0.007
RMSD bond angle	1.300
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.210
High resolution limit [Å]	2.100	2.100
Rmerge	0.062	0.301
Number of reflections	19129
<I/σ(I)>	8.6
Completeness [%]	95.0	87.1
Redundancy	2.9	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	293	18% 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 (%)