1AC5

CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1995-06
Detector	RIGAKU RAXIS II
Spacegroup name	P 21 21 21
Unit cell lengths	57.150, 83.050, 111.110
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 - 2.400
R-factor	0.195
Rwork	0.195
R-free	0.25000
Structure solution method	MIR, MOLECULAR REPLACEMENT
Starting model (for MR)	3sc2
RMSD bond length	0.006
RMSD bond angle	24.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.460
High resolution limit [Å]	2.400	2.400
Rmerge	0.051	0.154
Number of reflections	20693
<I/σ(I)>	18.1	6
Completeness [%]	91.9 *	81.2 *
Redundancy	5.11 *	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	6.5		used to seeding, Shilton, B.H., (1996) Protein Sci., 5, 395. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG5000	17 (%)
2	1	drop	protein	4 (mg/ml)
3	1	reservoir	ammonium acetate	400 (mM)
4	1	reservoir	glycerol	5 (%)