6XRV

X-ray structure of the monoclinic crystal form at 1.43 A resolution of lipase from Thermomyces (Humicola) lanuginosa at 173 K

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.3.1
Synchrotron site	ALS
Beamline	8.3.1
Temperature [K]	173
Detector technology	PIXEL
Collection date	2019-02-22
Detector	DECTRIS PILATUS 300K
Wavelength(s)	1.0
Spacegroup name	P 1 21 1
Unit cell lengths	76.929, 89.937, 123.422
Unit cell angles	90.00, 94.49, 90.00

Refinement procedure

Resolution	77.000 - 1.430
R-factor	0.1514
Rwork	0.149
R-free	0.18710
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tib
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	77.000	1.450
High resolution limit [Å]	1.430	1.430
Rmerge	0.158	5.690
Rmeas	0.163	6.100
Rpim	0.036	1.660
Number of reflections	307462	15076
<I/σ(I)>	9.1	0.4
Completeness [%]	99.7	98.8
Redundancy	19.2	13.3
CC(1/2)	0.998	0.260

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	295	Crystals grown by sitting drop with 0.6 ul reservoirs of 20% PEG 3350 in 0.1 M MES buffer at pH 6.5. Drops of 8 ul composed of equal amounts of the protein at 30.0 mg/ml in water with the reservoir solution. Room temperature throughout, crystals grew in about a month