issue contents

Journal logoBIOLOGICAL
ISSN: 1399-0047

October 2008 issue

Highlighted illustration

Cover illustration: Crystal-contact engineering of protein crystals, (p. 1020). A systematic study using the diphthine synthase system proved that a single mutation at crystal contact region can improve the diffraction quality of protein crystals. This figure shows an electron-density map around the mutation site of the K49R mutant which provided the best crystals at 1.5 Å resolution as compared with 2.1 Å of wild-type crystals.

research papers

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X-ray crystal structures have been obtained and molecular-dynamics simulations have been carried out for three active-site mutants (H48N, D49N and D49K) of bovine pancreatic phospholipase A2. The active site is disturbed in the Asp49 mutant structures.

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Three crystal structures of the γ-carbonic anhydrase enzyme from P. horikoshii were solved in space group F4132. The enzyme forms a β-helix and each trimer is stacked in a tetrahedral manner in the crystal.

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Crystal structures of the Ffh NG GTPase domain at < 1.24 Å resolution reveal multiple overlapping nucleotide binding modes.

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The influence of surfaces exposing ionizable groups on the crystallization of model proteins has been investigated.

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The crystal structure of an isolated unglycosylated antibody CH2 domain has been determined at 1.7 Å resolution.

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The crystal structure of PH1421, a phosphatase belonging to the haloacid dehalogenase superfamily, has been determined at 1.6 Å resolution. The structure reveals a dimeric state which may be important for the catalytic function of the enzyme.

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Peaks in the Patterson maps help in finding molecular positions in the unit cell and assist in molecular-replacement solution in difficult cases for molecules with helical pseudosymmetry.
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