6NKQ

The structure of bovine beta-lactoglobulin in novel crystals grown at pH 3.8

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	2018-02-12
Detector	DECTRIS PILATUS 300K
Wavelength(s)	.987
Spacegroup name	C 1 2 1
Unit cell lengths	65.888, 114.121, 140.506
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	57.060 - 2.300
R-factor	0.20974
Rwork	0.207
R-free	0.26097
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1beb
RMSD bond length	0.004
RMSD bond angle	1.109
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0238)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	60.000	2.700
High resolution limit [Å]	2.200	2.200
Rmerge	0.205	1.620
Rmeas	0.209	1.660
Rpim	0.031	0.240
Number of reflections	49538	2094
<I/σ(I)>	10.7	3.4
Completeness [%]	94.0	45.3
Redundancy	45.2	46.7
CC(1/2)	0.999	0.976

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	3.8	293	Reservoir of 3 M NaCl buffered with sodium citrate at pH 3.8 - heavy white precipitate formed upon mixing of 30 mg/ml protein in water with reservoir solution. Precipitate was removed by centrifugation. The clear remaining 12ul droplet was equilibrated against the reservoir for 12 to 60 hours