1BFK

CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN 40% ACETONITRILE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	296
Detector technology	IMAGE PLATE
Collection date	1997-11-19
Detector	RIGAKU RAXIS II
Spacegroup name	P 21 21 21
Unit cell lengths	79.038, 54.805, 53.928
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.300
R-factor	0.186
Rwork	0.186
R-free	0.24700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1scb
RMSD bond length	0.007
RMSD bond angle	27.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.400
High resolution limit [Å]	2.300	2.300
Rmerge	0.126 *	0.406 *
Total number of observations	34019 *
Number of reflections	10215	1098 *
<I/σ(I)>	10	3.9
Completeness [%]	93.7	85.9
Redundancy	3.3	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	5.6		PROTEIN WAS CRYSTALLIZED FROM 13% SODIUM SULFATE, 30 MM CACODYLATE, PH 5.6; THEN CROSS-LINKED WITH 10% GLUTARALDEHYDE IN 13% SODIUM SULFATE, 30 MM CACODYLATE, PH 7.5, WASHED WITH DISTILLED WATER, AND TRANSFERRED TO AN AQUEOUS SYSTEM CONTAINING 40% ACETONITRILE.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	cacodylate	330 (mM)
2	1	1	sodium sulfate	13 (%sat)