1B7H

OLIGO-PEPTIDE BINDING PROTEIN COMPLEXED WITH LYSYL-NORLEUCYL-LYSINE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Temperature [K]	120
Spacegroup name	P 21 21 2 A
Unit cell lengths	104.013, 74.078, 69.610
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.000
Rwork	0.210
R-free	0.26000
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.016
RMSD bond angle	0.037
Data reduction software	DENZO
Data scaling software	SCALA
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.000
Rmerge	0.086	0.390 *
Total number of observations	164050 *
Number of reflections	36776
<I/σ(I)>	6.8
Completeness [%]	99.3 *	98.2 *
Redundancy	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.5		pH 5.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	25 (mg/ml)
2	1	reservoir	PEG4000	7 (%)
3	1	reservoir	uranyl acetate	1 (mM)
4	1	reservoir	sodium acetate	50 (mM)