3LM1

Crystal Structure Analysis of Maclura pomifera agglutinin complex with p-nitrophenyl-GalNAc

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	CCD
Collection date	2000-06-30
Detector	ADSC QUANTUM 4r
Wavelength(s)	0.9793
Spacegroup name	P 21 21 21
Unit cell lengths	69.090, 133.290, 200.050
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.100
R-factor	0.223
Rwork	0.223
R-free	0.24400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1jot
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.800	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.039	0.290
Number of reflections	122330
<I/σ(I)>	24.7	4.5
Completeness [%]	83.8	46.6
Redundancy	3	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	298	0.5M of lithium sulfate, 12% PEG 8000, 1% octyl-beta-D-glucopyranoside, 0.1M Hepes, pH 7.0 in the reservoir solution. The sitting drop is made by protein (28mg/mL) and equal volumn of reservoir solution in the presence of p-nitrophenyl-alpha-GalNAc., VAPOR DIFFUSION, SITTING DROP, temperature 298K