2THF

STRUCTURE OF HUMAN ALPHA-THROMBIN Y225F MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Collection date	1998-04
Spacegroup name	P 21 21 21
Unit cell lengths	53.100, 75.100, 81.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 2.100
R-factor	0.199 *
Rwork	0.199
R-free	0.26500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ppb
RMSD bond length	0.010
RMSD bond angle	28.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.048	0.131
Total number of observations	68774 *
Number of reflections	18509
<I/σ(I)>	10	3.5
Completeness [%]	94.1	89.6
Redundancy	2.5	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5	20 *	mutants are inhibited by a 10-fold molar excess of H-D-Phe-Pro-Arg-chloromethylketone for 30 min at room temperature *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3.3 (mg/ml)
2	1	drop	MES	5 (mM)
3	1	drop		250 (mM)
4	1	reservoir	PEG8000	20 (%)
5	1	reservoir	zinc acetate	0.1 (M)
6	1	reservoir	cacodylate	0.1 (M)