1F6W

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12B
Synchrotron site	NSLS
Beamline	X12B
Temperature [K]	93
Detector technology	CCD
Collection date	1999-10-26
Detector	BRANDEIS - B4
Spacegroup name	P 21 21 21
Unit cell lengths	64.700, 88.970, 104.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.190 - 2.300
R-factor	0.212
Rwork	0.212
R-free	0.26700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1akn
RMSD bond length	0.011
RMSD bond angle	24.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.050	0.443
Number of reflections	25287
<I/σ(I)>	19.3	2.5
Completeness [%]	91.2	87.8
Redundancy	3.5	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	6.5	20 *	PEG 6000, NaCl, N-(2-acetamido) iminodiacetic acid, pH 6.5, EVAPORATION, temperature 293.K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	12 (%(w/v))
2	1	reservoir		100 (mM)
3	1	reservoir	ADA	100 (mM)