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- Publisher
- Wiley
- Copyright
- International Union of Crystallography, 2010
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309110010857
- pmid
- 20445263
- Publisher site
- See Article on Publisher Site
Abstract
6‐Hydroxymethyl‐7,8‐dihydropterin pyrophosphokinase (HPPK) catalyzes the Mg2+‐dependent transfer of pyrophosphate from ATP to 6‐hydroxymethyl‐7,8‐dihydropterin (HMDP), forming 6‐hydroxymethyl‐7,8‐dihydropterin pyrophosphate, which is a critical step in the de novo folic acid‐biosynthesis pathway. Diffraction‐quality crystals of HPPK from the medically relevant species Staphylococcus aureus were grown in the presence of ammonium sulfate or sodium malonate and diffracted to better than 1.65 Å resolution. The crystals belonged to space group P21, with unit‐cell parameters a = 36.8, b = 76.6, c = 51.5 Å, α = γ = 90.0, β = 100.2°. The crystals contained two molecules per asymmetric unit, with a volume per protein weight (VM) of 2.04 Å3 Da−1 and an estimated solvent content of 39.6%.
Journal
Acta Crystallographica Section F – Wiley
Published: May 1, 2010