1I6Q

Formation of a protein intermediate and its trapping by the simultaneous crystallization process: Crystal structure of an iron-saturated intermediate in the FE3+ binding pathway of camel lactoferrin at 2.7 resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	288
Detector technology	IMAGE PLATE
Collection date	2000-07-07
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	175.910, 80.620, 56.290
Unit cell angles	90.00, 92.37, 90.00

Refinement procedure

Resolution	25.000 - 2.700
R-factor	0.188
Rwork	0.188
R-free	0.25500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dtz
RMSD bond length	0.013 *
RMSD bond angle	1.800 *
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]	25.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.105	0.250
Total number of observations	44276 *
Number of reflections	19901
<I/σ(I)>	9.6	6.1
Completeness [%]	92.0	47
Redundancy	2.2	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICRODIALYSIS	8	4 *	ethanol, pH 8.0, MICRODIALYSIS, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	100 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)
3	1	reservoir	Tris-HCl	10 (mM)
4	1	reservoir	ethanol	26 (%(v/v))