6XOK

X-ray structure of the rhombohedral form of the lipase from Thermomyces lanuginosa at 1.3 A resolution

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	2019-02-20
Detector	DECTRIS PILATUS3 X CdTe 1M
Wavelength(s)	1.03
Spacegroup name	H 3 2
Unit cell lengths	76.373, 76.373, 241.551
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	80.000 - 1.300
R-factor	0.1056
Rwork	0.104
R-free	0.13430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ea6
RMSD bond length	0.008
RMSD bond angle	1.244
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.17.1_3660)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	80.000	1.330
High resolution limit [Å]	1.300	1.300
Rmerge	0.049	0.360
Rmeas	0.050	0.461
Rpim	0.008	0.205
Number of reflections	58358	463
<I/σ(I)>	42.7	2.6
Completeness [%]	88.0	14.4
Redundancy	31	4.2
CC(1/2)	1.000	0.810

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	298	Crystals were grown by vapor diffusion at room temperature in 24 well Cryschem sitting drop plates (Hampton Research, Aliso Viejo, CA) with 600 microleters reservoirs of 25% PEG 3350 in 0.10 M MES buffer at pH 6.5. The protein droplets were of 8ul volume and consisted of equal parts of a 20 to 30 mg/ml protein stock solution and the reservoir solution. Crystals usually appeared and grew to full size within one to two weeks. Rhombohedral crystals were thin needles of indeterminate cross-section