1VFE

HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY SER (R121S)

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995
Detector	RIGAKU RAXIS IIC
Spacegroup name	C 1 2 1
Unit cell lengths	97.900, 78.800, 58.900
Unit cell angles	90.00, 99.20, 90.00

Refinement procedure

Resolution	20.000 - 2.300
R-factor	0.196 *
Rwork	0.196
R-free	0.27000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1lct
RMSD bond length	0.011 *
RMSD bond angle	1.600 *
Data reduction software	AGROVATA/CCP4
Data scaling software	Agrovata
Phasing software	CCP4
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.300	2.300 *
Rmerge	0.086
Total number of observations	35914 *
Number of reflections	14539
Completeness [%]	73.8	47.5 *
Redundancy	2.47

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	8		50MM TRIS/HCL PH 8.0, 12% ISOPROPANOL

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	50-60 (mg/ml)
2	1	2	Tris-HCl	50 (mM)
3	1	2	2-propanol	12 (%)