8A28

Structure of the astacin zymogen of LAST-MAM from Limulus polyphemus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	CCD
Collection date	2010-04-18
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97244
Spacegroup name	C 1 2 1
Unit cell lengths	115.830, 47.570, 236.400
Unit cell angles	90.00, 102.91, 90.00

Refinement procedure

Resolution	46.730 - 2.400
R-factor	0.2538
Rwork	0.253
R-free	0.28860
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	AlphaFold
RMSD bond length	0.014
RMSD bond angle	1.260
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	BUSTER (2.10.4)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	76.800	2.540
High resolution limit [Å]	2.400	2.400
Rmerge	0.151	1.431
Rmeas	0.164	1.564
Number of reflections	49732	45644
<I/σ(I)>	9.8
Completeness [%]	99.6	98.6
Redundancy	6.4	6.1
CC(1/2)	0.995	0.594

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Optimal crystals of protein at ~6.8 mg/mL in 50 mM HEPES pH 7.0 were obtained at 20 degrees with 0.1 M bicine pH 9.0, 10% polyethylene glycol (PEG) 40,000, 2% dioxane as the reservoir solution.