3AL1

DESIGNED PEPTIDE ALPHA-1, RACEMIC P1BAR FORM

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	115
Detector technology	IMAGE PLATE
Collection date	1996-06-01
Detector	MARRESEARCH
Spacegroup name	P -1
Unit cell lengths	20.544, 20.859, 26.055
Unit cell angles	101.16, 97.03, 118.06

Refinement procedure

Resolution	18.000 - 0.750
R-factor	0.13
R-free	0.14500
Structure solution method	DIRECT METHODS
RMSD bond length	0.038
RMSD bond angle	0.000
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELXS
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	18.000	0.780
High resolution limit [Å]	0.750	0.750
Rmerge	0.100 *
Number of reflections	33573	1172 *
<I/σ(I)>	10.6	2
Completeness [%]	71.5	24.9
Redundancy	1.4	1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8		EQUAL VOLUMES OF 10 MG/ML D-ALPHA-1 AND 10 MG/ML L-ALPHA-1 WERE MIXED IMMEDIATELY BEFORE CRYSTALLIZATION. THE RESERVOIR SOLUTION CONTAINED 90-93% 2-METHYL-2,4-PENTANEDIOL, 0.075 M ETHANOLAMINE HCL PH 9.75, 0.05 M TRIETHANOLAMINE HCL PH 8. THE HANGING DROP CONTAINED EQUAL VOLUMES OF RESERVOIR AND 10 MG/ML D,L MIX ALPHA-1. THE ACIDIC PEPTIDE PARTWAY TITRATES THE BASIC BUFFERS TO REACH THE UNKNOWN RESULTANT PH., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	MPD	90-93 (%)
2	1	reservoir	ethanolamine-HCl	75 (mM)	pH9.75
3	1	reservoir	TEA-HCl	50 (mM)	pH8.0
4	1	drop	protein	10 (mg/ml)