1DTZ

STRUCTURE OF CAMEL APO-LACTOFERRIN DEMONSTRATES ITS DUAL ROLE IN SEQUESTERING AND TRANSPORTING FERRIC IONS SIMULTANEOUSLY:CRYSTAL STRUCTURE OF CAMEL APO-LACTOFERRIN AT 2.6A RESOLUTION.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1999-06-29
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	175.840, 80.920, 56.350
Unit cell angles	90.00, 92.35, 90.00

Refinement procedure

Resolution	11.940 - 2.650
R-factor	0.198
Rwork	0.198
R-free	0.26600
RMSD bond length	0.013
RMSD bond angle	2.500
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.700
High resolution limit [Å]	2.600	2.600
Rmerge	0.078 *	0.250 *
Number of reflections	22549
<I/σ(I)>	9.1
Completeness [%]	98.0	91
Redundancy	2.98	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICRODIALYSIS	8	277	TRIS HCl ETHANOL TRISODIUM CITRATE, pH 8.0, MICRODIALYSIS, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	100 (mg/ml)
2	1	1	Tris-HCl	10 (mM)
3	1	2	ethanol	24 (%(v/v))