9S6M

Structure of BFL1 in complex with a covalent inhibitor, alternative series, cmpd25

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-10-03
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.95372
Spacegroup name	P 1 21 1
Unit cell lengths	56.634, 43.382, 62.055
Unit cell angles	90.00, 93.63, 90.00

Refinement procedure

Resolution	61.930 - 1.427
R-factor	0.1954
Rwork	0.194
R-free	0.21430
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	0.980
Data reduction software	autoPROC (autoPROC 1.0.5 (20220608))
Data scaling software	STARANISO (2.3.87 (20220518))
Phasing software	PHASER (2.8.3)
Refinement software	BUSTER (2.11.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	61.930	1.546
High resolution limit [Å]	1.427	1.427
Rmerge	0.056	0.812
Rmeas	0.063	0.909
Rpim	0.027	0.407
Number of reflections	43147	2159
<I/σ(I)>	12.8	1.6
Completeness [%]	76.9	18.2
Redundancy	5	4.9
CC(1/2)	0.999	0.683

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Crystallization of adducted protein was carried out using a 2D optimization grid, (sodium citrate 0.6-1.1 M, vs PCTP buffer, 0.1 M pH 4.5-9.5). 300 nL drops (150 nL protein, 150 nL mother liquor) were incubated at 293 K in a sitting drop vapour diffusion format, dispensed using a Mosquito (SPT Labtech) and SWISSCI MRC 2-drop plates