Preliminary X-ray diffraction studies of recombinant 19 kDa human fibroblast collagenase.

Abstract:

:Crystals of the catalytic domain of human fibroblast collagenase have been grown in the presence and absence of an inhibitor. Crystals of the inhibitor complex grew from 0.2 M ammonium sulfate and 15 to 30% PEG 8000 at 22 degrees C as bipyramids in the space group P6(2) or P6(4). Crystals of the unligated enzyme grew as rods in the space group P4(1)2(1)2 or P4(3)2(1)2 from 1.0 to 2.0 M sodium formate at 4 degrees C. Both crystal forms grew quite slowly over a period of months, but ultimately yielded crystals that diffracted beyond 2.5 A. The collagenase samples used in these studies were heterogeneous at the amino terminus. Three major species (full length, N-1 and N-2) were identified by mass spectrometry and Edman sequencing. Analysis of dissolved crystals revealed the native crystal form selectively crystallized as the N-2 species; however, no selectivity of N-terminal forms was observed for crystals of the inhibitor complex.

journal_name

J Mol Biol

authors

Hassell AM,Anderegg RJ,Weigl D,Milburn MV,Burkhart W,Smith GF,Graber P,Wells TN,Luther MA,Jordan SR

doi

10.1016/0022-2836(94)90068-x

subject

Has Abstract

pub_date

1994-03-11 00:00:00

pages

1410-2

issue

5

eissn

0022-2836

issn

1089-8638

pii

0022-2836(94)90068-X

journal_volume

236

pub_type

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