issue contents

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047

March 2001 issue

Highlighted illustration

Cover illustration: Crystal contacts mapped on the solvent-accessible surface of E. coli L-asparaginase, an enzyme used for cancer therapy (p. 369).

research papers


link to html
The M148Q mutant of rusticyanin crystallizes with two molecules per asymmetric unit which shows a potential electron transfer route and redox partner docking site.

link to html
The crystal structures of a peptidyl-Lys metalloendopeptidase from G. frondosa were solved in four crystal forms. The structure belongs to a new `aspzincin` family with a novel active-site architecture.

link to html
The structures of the Y25F mutant of E. coli L-asparaginase and of native E. chrysanthemi L-asparaginase with quasi-enantiomorphic crystals obtained in the hexagonal space groups P6522 and P6122, respectively, are compared.

link to html
The structure of glycosylated fibroblast growth factor 9 has been determined at 2.6 Å resolution. FGF9 forms dimers with most of the receptor-binding residues buried in the dimer interface.

link to html
Anisotropic refinement at near-atomic resolution clarifies primary sequence discrepancies and reveals new structural details of the T. aurantiacus xylanase I.

link to html
The molecular structure of the ternary complex of S. cerevrisiae Nmt1p with a bound non-hydrolyzable myristoyl-CoA analog and a competitive peptidomimetic inhibitor has been solved to 2.9 Å.

link to html
For the metals Ca, Mg, Mn, Fe, Cu and Zn, geometry determined in high-resolution metalloprotein structures is compared with that in appropriate small-molecule complexes in the Cambridge Structural Database. Targets for refinement and for validation of distances and angles around the metal are proposed and unusual features of zinc carboxylate geometry highlighted.

link to html
Interferometric study on the development of concentration-depletion zones around protein crystals growing in microgravity and gelled on-ground experiments.

crystallization papers


link to html
The dihaem cytochrome NapB of H. influenzae was overexpressed, purified and crystallized. Native X-ray diffraction data were collected to 1.8 Å resolution using synchrotron radiation.

link to html
The crystallization and preliminary diffraction data analysis for the complex of an 15N-­labelled mutant form of RTP and a symmetrical form of its DNA-binding site is reported.

link to html
Crystals of anthocyanidin synthase from A. thaliana, a non-haem iron(II)-dependent dioxygenase involved in pigment production in higher plants, have been obtained both aerobically and anaerobically, and shown to diffract to 2.4 Å.

link to html
Recombinant P. furiosus prolidase, a dipeptide-specific proline aminopeptidase, has been crystallized in two forms. Laboratory and synchrotron data have been recorded.

link to html
Human betaine–homocysteine S-methyltransferase was cloned, expressed in E. coli, purified and crystallized. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 109.190, b = 91.319, c = 88.661 Å, β = 122.044°, and diffract to 2.9 Å.

link to html
The stoechiometric complex between the human RXRα ligand binding domain and 9-cis retinoic acid, its natural ligand, has been purified and crystallized in a tripartite mixture of sodium formate, glycerol and propane diol.

link to html
RNase HIII from B. subtilis has been overexpressed and crystallized. X-ray diffraction data have been collected to 2.8 Å resolution using synchrotron radiation.

link to html
A transcription-factor complex consisting of four different polypeptides and a DNA duplex has been assembled from purified components and crystallized. Diffraction data have been collected to 3.6 Å resolution.

link to html
NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase has been crystallized in the presence and absence of its reaction substrate and product and 1.65 Å resolution data have been collected.

link to html
The periplasmic binding protein ProX from E. coli has been crystallized with bound ligands (glycine betaine and proline betaine) and yields data to 1.9 Å resolution.

link to html
Glycerol-3-phosphate 1-acyltransferase from squash has been crystallized by the hanging-drop method of vapour diffusion using PEG 4000 as the precipitant. Preliminary data collected to 1.9 Å resolution have identified that these crystals are most likely to belong to space group P212121 with unit-cell parameters a = 61.1, b = 65.1, c= 103.3 Å and α = β = γ = 90°

link to html
Fructose-1,6-/sedoheptulose-1,7-bisphosphatase of Synechococcus PCC 7942 has been purified and crystallized. The crystals belong to the monoclinic space group P21 with unit-cell parameters a = 80.1, b = 84.2, c = 104.3 Å and β = 101.7°.

link to html
Polymethoxygalacturonase SX1 from T. penicillatum was crystallized and diffracted to 2.08 Å resolution. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 165.6, b = 61.0, c = 48.7 Å, β = 93.1°.

link to html
Forkhead-associated (FHA) domains of the cell-cycle checkpoint protein kinases Dun1p and Rad53p have been crystallized and X-ray diffraction data have been collected to 3.1 and 4.0 Å resolution, respectively.

link to html
The preliminary structure of an antibody (Fab41.4) that inhibits activating transcription factor 1 (ATF-1) from binding to a specific DNA sequence (CRE) is presented.

link to html
Orthogonal crystals of the human pyruvate dehydrogenase (E1) have been obtained. A native data set, complete to 2.5 Å has been collected.

link to html
A protein belonging to the Lrp/AsnC family from the hyperthermophilic archaeon Pyrococcus sp. OT3 was crystallized. In the crystal, a dimer is formed by two sets of four β-strands; the resultant dimers further associate.

short communications


link to html
A 3.1 Å structure of HIV-1 protease in complex with a peptidomimetic inhibitor reveals the hydrogen-bonding pattern between active-site aspartic acids and the hydroxyethylamine transition-state analogue.

book reviews


Acta Cryst. (2001). D57, 477
doi: 10.1107/S090744490001982X

Acta Cryst. (2001). D57, 478
doi: 10.1107/S0907444900013743

books received


Acta Cryst. (2001). D57, 478
doi: 10.1107/S0907444900014335
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds