1B3E

HUMAN SERUM TRANSFERRIN, N-TERMINAL LOBE, EXPRESSED IN PICHIA PASTORIS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1996-05
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 41 21 2
Unit cell lengths	73.500, 73.500, 156.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 2.500
R-factor	0.177 *
Rwork	0.177
R-free	0.25500
Structure solution method	OTHER
Starting model (for MR)	1A8F (HUMAN TRANSFERRIN N-LOBE)
RMSD bond length	0.010
RMSD bond angle	1.800
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.066	0.245
Number of reflections	15238
<I/σ(I)>	17	4.2
Completeness [%]	96.9	96
Redundancy	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.25	4 *	PROTEIN WAS CRYSTALLIZED FROM 40% (V/V) ETHANOL WITH 50MM SODIUM CACODYLATE, PH 6.25. GROWN IN SITTING DROPS AT 277 K. RESERVOIRS CONTAINED 40% (V/V) ETHANOL, 50MM SODIUM CACODYLATE, PH 5.8 - 6.3. PRIOR TO CRYSTALLIZATION, THE PROTEIN WAS DIALYSED AGAINST SODIUM BICARBONATE, PH 8.1, VAPOR DIFFUSION, SITTING DROP, temperature 277.0K

Crystallization Reagents

ID	crystal ID	solution ID	reagent name	concentration	details
1	1	2	40% (V/V) ETHANOL WITH 50MM SODIUM CACODYLATE, PH 6.25.
2	1	2	0% (V/V) ETHANOL, 50MM SODIUM CACODYLATE,PH 5.8 - 6.3.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	80 (mg/ml)
2	1	drop	sodium bicarbonate	150 (mM)
3	1	reservoir	ethanol	40 (%(v/v))
4	1	reservoir	sodium cacodylate	50 (mM)