1B7U

Structure of Mare Apolactoferrin: the N and C Lobes are in the Closed Form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-08-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	100.400, 77.400, 102.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.000 - 3.800
Rwork	0.200
R-free	0.30000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	DIFERRIC MARE LACTOFERRIN
RMSD bond length	0.016
RMSD bond angle	24.700 *
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]	32.000
High resolution limit [Å]	3.800	3.800 *
Rmerge	0.150
Total number of observations	101096 *
Number of reflections	7887
<I/σ(I)>	14
Completeness [%]	99.2	98.6 *
Redundancy	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Microdialysis *	8.5	277 *	pH 8.5, VAPOR DIFFUSION, HANGING DROP

Crystallization Reagents

ID	crystal ID	solution ID	reagent name	concentration	details
1	1	1	TRIS-HCL
2	1	2	METHANOL
3	1	2	TRIS-HCL

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1		protein	40-50 (mg/ml)
2	1	1	Tris-HCl	0.01 (M)
3	1		Tris-HCl	0.01 (M)
4	1	2	ethanol	10 (%(v/v))