1E1H

Crystal Structure of recombinant Botulinum Neurotoxin Type A Light Chain, self-inhibiting Zn endopeptidase.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	125
Detector technology	CCD
Collection date	2000-01-15
Detector	ADSC CCD
Spacegroup name	P 1 21 1
Unit cell lengths	58.064, 94.263, 100.156
Unit cell angles	90.00, 103.52, 90.00

Refinement procedure

Resolution	19.340 - 1.800
Rwork	0.196
R-free	0.23700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	LC COORDINATES OF PDB ENTRY 3BTA
RMSD bond length	0.020
RMSD bond angle	1.850 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	EPMR
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.340	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.042 *	0.383 *
Number of reflections	93168	6918 *
<I/σ(I)>	7.9	1.7
Completeness [%]	95.2	95.2
Redundancy	3.3 *	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	22 *	HANGING DROP VAPOUR DIFFUSION, DROP: 4UL 5MG/ML PROTEIN & 2UL WELL. PROTEIN: 0.05M TRIS PH 8.0,10% GLYCEROL, 0.1% TRITON X-100,1.0MM 2-ME,4% XYLITOL. WELL: 0.2M (NH4)2SO4,0.1M NAOAC PH 4.6, 25% PEG4000.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	drop	triton X-100	0.1 (%)
3	1	drop	Tris	25 (mM)	pH8.0
4	1	drop	glycerol	10 (%(v/v))
5	1	drop	MPD	1 (mM)
6	1	reservoir	ammonium sulfate	0.2 (M)
7	1	reservoir	sodium acetate	0.1 (M)	pH4.6
8	1	reservoir	PEG4000	25 (%(w/v))
9	1	reservoir	xylitol	3 (%)