1GZ7

Crystal structure of the closed state of lipase 2 from Candida rugosa

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	120
Detector technology	CCD
Collection date	2001-05-15
Spacegroup name	P 1
Unit cell lengths	61.150, 91.140, 108.460
Unit cell angles	90.78, 106.31, 86.91

Refinement procedure

Resolution	12.000 * - 1.970
R-factor	0.2
Rwork	0.200
R-free	0.23000 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1trh
RMSD bond length	0.006
RMSD bond angle	23.200 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	37.110	2.080
High resolution limit [Å]	1.970	1.970
Rmerge	0.100 *	0.300 *
Total number of observations	299637 *
Number of reflections	152503
<I/σ(I)>	4.6	2.2
Completeness [%]	94.6	76.5
Redundancy	2	1.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5 *	291 *	15% (W/V) PEG 4000, SODIUM ACETATE 0.1M, PH 5.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	15 (%(w/v))
2	1	reservoir	sodium acetate	0.1 (M)	pH5.0
3	1	drop	protein	7-8 (mg/ml)