1BGP

CRYSTAL STRUCTURE OF BARLEY GRAIN PEROXIDASE 1

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	287
Detector technology	IMAGE PLATE
Collection date	1994-03
Detector	RIGAKU
Spacegroup name	P 21 21 2
Unit cell lengths	71.920, 105.060, 40.950
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.000 - 1.900
R-factor	0.192
Rwork	0.192
R-free	0.23000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1sch POLY-ALA CHAIN
RMSD bond length	0.004
RMSD bond angle	19.700 *
Data reduction software	DENZO
Data scaling software	CCP4
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.000	1.990
High resolution limit [Å]	1.900	1.900
Rmerge	0.088 *	0.416 *
Total number of observations	140862 *
Number of reflections	24371
<I/σ(I)>	7.4	1.8
Completeness [%]	96.8	81.4
Redundancy	5.8	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		Henriksen, A., (1992) J. Mol. Biol., 228, 690. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG6000	20 (%)
3	1	reservoir	potassium phosphate	0.01 (M)