1FBL

STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVEALS A C-TERMINAL DOMAIN CONTAINING A CALCIUM-LINKED, FOUR-BLADED BETA-PROPELLER

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1994-10-11
Detector	MAR scanner 300 mm plate
Spacegroup name	I 41
Unit cell lengths	161.140, 161.140, 52.220
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	9.000 - 2.500
R-factor	0.217
Rwork	0.217
RMSD bond length	0.015
RMSD bond angle	26.300 *
Data reduction software	MOSFLM
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.200
High resolution limit [Å]	2.500
Rmerge	0.086	0.230 *
Total number of observations	72655 *
Number of reflections	22212
Completeness [%]	94.2	66.7 *
Redundancy	3.27

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.3 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG	5 (%(w/v))
2	1	reservoir		10 (mM)