Crystallization and preliminary X-ray diffraction analysis of two N-terminal fragments of the DNA-cleavage domain of topoisomerase IV from Staphylococcus aureus

Carr, S.B.; Makris, G.; Phillips, S.E.V.; Thomas, C.D.

doi:10.1107/S1744309106044150

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
(a) A monoclinic crystal of GrlA56; typical dimensions are 400 × 300 × 20 µm. (b) An orthorhombic crystal of GrlA59 mounted in a cryoloop prior to data collection; typical dimensions are 500 × 150 × 20 µm.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 62| Part 11| October 2006| Pages 1164-1167

doi:10.1107/S1744309106044150

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