1H54

Maltose phosphorylase from Lactobacillus brevis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE D41A
Synchrotron site	LURE
Beamline	D41A
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	83.750, 102.500, 114.000
Unit cell angles	90.00, 111.30, 90.00

Refinement procedure

Resolution	29.100 - 2.150
R-factor	0.173 *
Rwork	0.186
R-free	0.21400 *
Structure solution method	MIR
RMSD bond length	0.005
RMSD bond angle	23.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.350
High resolution limit [Å]	2.150	2.150
Rmerge	0.076 *
Number of reflections	95868
<I/σ(I)>	23	7.7
Completeness [%]	98.2	95.7
Redundancy	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6		O.1 M CITRATE, 0.03M PHOSPHATE; PH 6.0, 20% POLY ACRYLIC ACID 20000

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8-10 (mg/ml)
2	1	drop	citrate	10 (mM)
3	1	reservoir	PAA20000	18 (%)
4	1	reservoir	citrate	0.1 (M)
5	1	reservoir	phosphate	0.03 (M)