Loading…
Crystallization and preliminary X-ray diffraction analysis of proline iminopeptidase from Xanthomonas campestris pv. citri
Proline iminopeptidase from Xanthomonas campestris pv. citri, displaying no significant sequence homology to any protein previously analyzed by X-ray crystallography, has been crystallized using the vapour diffusion method. Two different orthorhombic crystal forms (space group C222 and I222) were ob...
Saved in:
Published in: | FEBS letters 1997-01, Vol.400 (1), p.91-93 |
---|---|
Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | Proline iminopeptidase from
Xanthomonas campestris pv.
citri, displaying no significant sequence homology to any protein previously analyzed by X-ray crystallography, has been crystallized using the vapour diffusion method. Two different orthorhombic crystal forms (space group C222 and I222) were obtained from a solution containing NaCl or polyethylene glycol monomethyl ether (MW 5000) as precipitating agent for the native and lanthanum-derivatized protein, respectively. Complete diffraction data sets have been collected up to 2.6 Å (native) and 3.0 Å (lanthanum derivative) resolution. Cell dimensions are
a=147.2 Å,
b=167.8 Å, and
c=85.6 Å (C222) and
a=146.7 Å,
b=167.7 Å, and
c=171.4 Å (I222), respectively. Considerations of the possible values of
V
m and analysis of the self-rotation function of the native crystals account for the presence of one dimer per asymmetric unit, whereas a tetramer probably would occupy the smallest crystallographically independent crystal portion in the lanthanum-derivatized protein crystals. |
---|---|
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/S0014-5793(96)01363-4 |