37DS

Crystal Structure of Thermomyces lanuginosa Lipase With Bound 1,3 diacylglycrol and Fatty Acid Acyl intermediates: Monoclinic Crystals

Replaces:  6XRV

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	2024-12-19
Detector	DECTRIS EIGER X 16M
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	76.690 - 1.430
R-factor	0.1326
Rwork	0.130
R-free	0.18110
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.012
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.21.1_5286)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	77.000	1.470
High resolution limit [Å]	1.430	1.430
Rmerge	0.158	5.690
Rmeas	0.163	6.100
Rpim	0.360	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	5.5	298	Crystallized by sitting drop vapor diffusion with 0.6 ml reservoirs and drop volumes 6 ul. Drops consisted of equal volumes of the reservoir and the protein stock solution. The reservoirs were 20% w/v PEG 3350 with 0.1 M HEPES buffer. The protein was in the growth broth of the aspergillum expression system and was not further purified. The stock protein concentration was 30 mg/ml