1B1X

STRUCTURE OF DIFERRIC MARE LACTOFERRIN AT 2.62A RESOLUTION

Replaces:  1BGR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	288
Detector technology	IMAGE PLATE
Collection date	1997-03-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	85.175, 99.496, 103.052
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.620
R-factor	0.194 *
Rwork	0.194
R-free	0.26400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	HUMAN LACTOFERRIN
RMSD bond length	0.012
RMSD bond angle	2.000
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.780
High resolution limit [Å]	2.620	2.620
Rmerge	0.063	0.250
Number of reflections	25558
<I/σ(I)>	28.7	5.29
Completeness [%]	95.3	80 *
Redundancy	3.87	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	8.5	6 *	40MG/ML PROTEIN IN 10MM TRIS HCL, PH 8.5, MICRODIALYSED AGA AT 6 DEGREES CELSIUS

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	20-30 (mg/ml)
2	1	1	Tris-HCl	0.025 (M)
3	1	2	ethanol	10 (%(v/v))