1BJR

COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATED LACTOFERRIN FRAGMENT AND PROTEINASE K

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	288
Detector technology	IMAGE PLATE
Collection date	1997-02
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	44.600, 38.581, 79.220
Unit cell angles	90.00, 105.80, 90.00

Refinement procedure

Resolution	12.000 - 2.440
R-factor	0.167
Rwork	0.160
R-free	0.22500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3prk
RMSD bond length	0.008
RMSD bond angle	0.021
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CCP4

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	12.000	2.570
High resolution limit [Å]	2.440	2.440
Rmerge	0.070	0.168
Total number of observations	23005 *
Number of reflections	9051
<I/σ(I)>	22.2	9.7
Completeness [%]	92.2	80.9
Redundancy	2.42	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICRODIALYSIS	6	279	60 MG/ML PROTEIN IN 10MM TRIS.HCL, PH 6.0 WAS MICRODIALYZED AGAINST 10% ETHANOL AT 6 DEGREE CELSIUS, microdialysis, temperature 279K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	30 (mg/ml)
2	1	2	ethanol	10 (%)