Biological Crystallography

 

Acta Cryst. (2002). D58, 1765-1771  [ doi:10.1107/S0907444902011642 ]

Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase

C. E. Felder, M. Harel, I. Silman and J. L. Sussman

Synopsis: The X-ray structure of the complex of BW284C51 with T. californica acetylcholinesterase was determined at 2.85  Å resolution and compared with the structures of complexes of the same enzyme with two other active-site gorge-spanning inhibitors, viz decamethonium and E2020.

PDB reference: 1e3q

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1772-1779  [ doi:10.1107/S0907444902011678 ]

Substructure solution with SHELXD

T. R. Schneider and G. M. Sheldrick

Synopsis: The application of the SHELXD program to the location of heavy-atom sites from MAD or SAD data is illustrated with the help of examples.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1780-1786  [ doi:10.1107/S0907444902012222 ]

Physical estimation of triplet phases from two new proteins

F. Mo, R. H. Mathiesen, P. M. Alzari, J. Lescar and B. Rasmussen

Synopsis: Triplet phases have been obtained for three new proteins from three-beam diffraction. A brief discussion of strategies for the collection of triplet phases and their application in macromolecular crystallography is given.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1787-1792  [ doi:10.1107/S0907444902012234 ]

Comparison of the refined crystal structures of wild-type (1.34  Å) flavodoxin from Desulfovibrio vulgaris and the S35C mutant (1.44  Å) at 100  K

R. Artali, G. Bombieri, F. Meneghetti, G. Gilardi, S. J. Sadeghi, D. Cavazzini and G. L. Rossi

Synopsis: The structure at 100  K (synchrotron radiation) of the S35C mutant of D. vulgaris flavodoxin at 1.44  Å resolution has been compared with the refined wild-type (wt) structure at 1.34  Å resolution. A different orientation of the Cys35 thiol group with respect to the Ser35 hydroxyl has been found.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1793-1802  [ doi:10.1107/S0907444902013069 ]

Secondary structures at polypeptide-chain termini and their features

R. Bhattacharyya, D. Pal and P. Chakrabarti

Synopsis: An analysis of length and residue distributions, interactions and location in the overall tertiary structure of -helices and -strands at polypeptide-chain termini is presented and discussed in the context of protein folding and design.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1803-1812  [ doi:10.1107/S090744490201329X ]

Structural analysis of the two horseradish peroxidase catalytic residue variants H42E and R38S/H42E: implications for the catalytic cycle

K. Meno, S. Jennings, A. T. Smith, A. Henriksen and M. Gajhede

Synopsis: The crystal structures of two mutants of horseradish peroxidase C (HRPC) with substitutions of the key catalytic residues Arg83 and His42 have been determined to 2.5  Å (H42E HRPC) and 2.0  Å (R38S/H42E HRPC) resolution.

PDB references: 4atj and 1kzm

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1813-1819  [ doi:10.1107/S0907444902013720 ]

Design of specific peptide inhibitors of phospholipase A₂: structure of a complex formed between Russell's viper phospholipase A₂ and a designed peptide Leu-Ala-Ile-Tyr-Ser (LAIYS)

V. Chandra, J. Jasti, P. Kaur, S. Dey, A. Srinivasan, Ch. Betzel and T. P. Singh

Synopsis: The structure of the complex formed between Russell's viper phospholipase A₂ and a designed peptide LAIYS has been determined at 2.0  Å resolution. The peptide binds to phospholipase A₂ specifically and fills the hydrophobic channel completely.

PDB reference: 1jq8

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1820-1825  [ doi:10.1107/S0907444902013707 ]

On the fitting of model electron densities into EM reconstructions: a reciprocal-space formulation

J. Navaza, J. Lepault, F. A. Rey, C. Álvarez-Rúa and J. Borge

Synopsis: A fast method for fitting model electron densities into EM reconstructions is presented. This new procedure was inspired by a rigid-body refinement method used in macromolecular X-ray crystallography.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1826-1829  [ doi:10.1107/S0907444902010910 ]

Purification, crystallization and preliminary X-ray analysis of the BRCT domains of human 53BP1 bound to the p53 tumour suppressor

D. J. Derbyshire, B. P. Basu, T. Date, K. Iwabuchi and A. J. Doherty

Synopsis: To investigate how the BRCT domains of 53BP1 protein bind to p53, the 53BP1 BRCT region in complex with the DNA-binding domain of p53 was overexpressed, purified and crystallized. The crystals of the complex belong to the space group P2₁2₁2₁ and diffraction data have been collected to 2.6  Å resolution.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1830-1832  [ doi:10.1107/S0907444902013331 ]

Crystallization and preliminary X-ray characterization of archaeal group II chaperonin -subunit from Thermococcus strain KS-1

Y. Shomura, T. Yoshida, T. Maruyama, M. Yohda and K. Miki

Synopsis: The mutant -subunit of group II chaperonin from Thermococcus strain KS-1 was crystallized. Diffraction data were collected to 2.4  Å with a synchrotron-radiation source.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1833-1835  [ doi:10.1107/S0907444902014701 ]

Purification, crystallization and preliminary X-ray diffraction analysis of a novel mannose-binding lectin from Gastrodia elata with antifungal properties

W. Liu, Y.-L. Hu, M. Wang, Y. Xiang, Z. Hu and D.-C. Wang

Synopsis: A plant antifungal protein, Gastrodia antifungal protein (GAFP-1) has been purified from terminal corms of the orchid G. elata and crystallized in space group P2₁2₁2 and with unit-cell parameters a = 61.087, b = 91.488, c = 81.132  Å. A set of diffraction data to resolution 2  Å has been collected with an overall R_merge of 0.097 and a completeness of 99.8%, which will help to solve the first structure of a monomeric monocot mannose-binding lectin.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1836-1837  [ doi:10.1107/S0907444902011654 ]

Preliminary crystallographic study of an acidic phospholipase A₂ from Ophiophagus hannah (king cobra)

S. Xu, L. Gu, Q. Wang, Y. Shu and Z. Lin

Synopsis: A non-toxic acidic phospholipase A₂ from the venom of O. hannah (king cobra) has been crystallized and X-ray data have been collected and reduced to 2.1  Å resolution. Analysis by molecular replacement showed there to be six enzyme molecules per asymmetric unit.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1838-1840  [ doi:10.1107/S0907444902012131 ]

Crystallization and preliminary crystallographic studies of a novel antifungal protein with five disulfide bridges from Eucommia ulmoides Oliver

Y. Xiang, R.-H. Huang, W. Liu, G.-P. Li, X.-Z. Liu and D.-C. Wang

Synopsis: A novel antifungal protein with five disulfide bridges from E. ulmoides Oliver has been crystallized. X-ray diffraction data at 1.0  Å have been collected and used to obtain phase information directly by an ab initio method.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1841-1842  [ doi:10.1107/S0907444902012155 ]

Crystallization and preliminary X-ray diffraction analysis of recombinant hydrolase domain of 10-formyltetrahydrofolate dehydrogenase

A. A. Chumanevich, C. Davies and S. A. Krupenko

Synopsis: 10-Formyltetrahydrofolate dehydrogenase is important for the regulation of intracellular folate pools, for de novo purine biosynthesis and for the removal of formate in the form of CO₂. Crystals of the amino-terminal hydrolase domain of this enzyme that diffract to 2.3  Å resolution have been obtained.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1843-1845  [ doi:10.1107/S0907444902012325 ]

Crystallization and preliminary crystallographic characterization of the extracellular Ig-like domain of human natural killer cell activating receptor NKp44

C. Cantoni, M. Ponassi, R. Biassoni, R. Conte, A. Spallarossa, A. Moretta, L. Moretta, M. Bolognesi and D. Bordo

Synopsis: NKp44, a natural killer cell activating receptor, is composed of an extracellular region (168 amino acids), a membrane-spanning segment (25 amino acids) and a cytoplasmic domain (63 amino acids). The extracellular region Ig-like domain, held to be involved in target-cell recognition/binding, has been crystallized in a form suitable for structural investigation.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1846-1847  [ doi:10.1107/S0907444902012611 ]

Crystallization and preliminary X-ray analysis of cyclophilin from Leishmania donovani

R. Banerjee, M. Dutta, M. Sen and A. K. Datta

Synopsis: Cyclophilin from the parasite L. donovani has been crystallized, with crystals diffracting up to 3.5  Å resolution. Unambiguous solutions in rotation and translation functions have been obtained with human cyclophilin as the search model.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1848-1850  [ doi:10.1107/S090744490201260X ]

Human neuroglobin: crystals and preliminary X-ray diffraction analysis

A. Pesce, M. Nardini, S. Dewilde, P. Ascenzi, T. Burmester, T. Hankeln, L. Moens and M. Bolognesi

Synopsis: Human neuroglobin (151 amino acids), a haemoglobin involved in the neuronal response to hypoxia or ischaemia, has been expressed, purified and crystallized as a Cys-free mutant protein, with a view to three-dimensional structure determination.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1851-1853  [ doi:10.1107/S0907444902012970 ]

Expression, purification and crystallization of Dpr, a ferritin-like protein from the Gram-positive meningitis-associated bacterium Streptococcus suis

S. Haataja, A. Penttinen, A. T. Pulliainen, K. Tikkanen, J. Finne and A. C. Papageorgiou

Synopsis: Dpr, a ferritin-like protein from S. suis, was expressed in E. coli, purified and crystallized. Full data were collected to 2.3  Å resolution using synchrotron radiation.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1854-1857  [ doi:10.1107/S0907444902013288 ]

Cloning, purification and crystallization of full-length human annexin 2

J. T. Tran, A. Rosengarth and H. Luecke

Synopsis: Crystallization and preliminary diffraction data analysis for recombinant human annexin 2 to 1.52  Å resolution.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1858-1861  [ doi:10.1107/S0907444902013306 ]

Crystallization of cyclase-associated protein from Dictyostelium discoideum

A. Hofmann, S. Hess, A. A. Noegel, M. Schleicher and A. Wlodawer

Synopsis: Cyclase-associated protein (CAP) from D. discoideum, a protein involved in signal transduction, has been crystallized and a complete native data set has been collected at 2.2  Å resolution.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1862-1864  [ doi:10.1107/S090744490201332X ]

Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the transcriptional activator protein PhoB from Escherichia coli

K. Shindoh, K. Maenaka, T. Akiba, H. Okamura, Y. Nishimura, K. Makino and Y. Shirakihara

Synopsis: The DNA-binding domain of the transcriptional activator PhoB (PhoBC) has been expressed in E. coli and crystallized in two crystal forms, one of which led to experimental maps at 3.0  Å resolution.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1865-1867  [ doi:10.1107/S0907444902013963 ]

Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein

K. M. Pos and K. Diederichs

Synopsis: The multi-drug efflux transporter AcrB from E. coli was purified and crystallized. AcrB crystallizes in space group R32, with unit-cell parameters a = b = 143, c = 513  Å. Crystals diffract to 3.0  Å resolution.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1868-1870  [ doi:10.1107/S0907444902013719 ]

Expression, purification, crystallization and preliminary X-ray analysis of the sexual stage-specific protein Pfg27 from Plasmodium falciparum

S. Kumar Singh, S. Prasad Sati, D. Kongkasuriyachai, N. Kumar and A. Sharma

Synopsis: To aid studies in understanding gametocytogenesis in P. falciparum, Pfg27 has been expressed and purified yielding 5  mg  l^-1 of purified protein in soluble form. This protein has been crystallized by the hanging-drop vapor diffusion method using PEG 8000 as a precipitant. Native diffraction data were collected under cryogenic conditions, and phase resolution by selenium-methionine aided multiple-wavelength anomalous dispersion technique is in progress.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1871-1873  [ doi:10.1107/S090744490201380X ]

Preparation of a crystallizable mRNA-binding fragment of Moorella thermoacetica elongation factor SelB

M. Selmer, R. Wilting, D. Holmlund and X.-D. Su

Synopsis: A C-terminal 30  kDa fragment of the selenocysteine-specific elongation factor SelB from M. thermoacetica has been recloned, expressed in E. coli and crystallized in a suitable form for X-ray analysis. The crystals diffract to 2.7  Å in an in-house X-ray source.

PDB reference: 1lva

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1874-1875  [ doi:10.1107/S0907444902013835 ]

Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Pseudomonas aeruginosa

H.-W. Kim, B. W. Han, H.-J. Yoon, J. K. Yang, B. I. Lee, H. H. Lee, H. J. Ahn and S. W. Suh

Synopsis: Peptide deformylase from P. aeruginosa has been crystallized (P2₁2₁2₁; a = 68.75, b = 74.46, c = 77.18  Å). Diffraction data have been collected to 1.85  Å using synchrotron X-rays.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1876-1878  [ doi:10.1107/S0907444902013860 ]

Purification, crystallization and preliminary X-ray diffraction analysis of yeast nucleosome-assembly factor Cia1p

B. Padmanabhan, K. Kataoka, N. Adachi and M. Horikoshi

Synopsis: The nucleosome-assembly factor Cia1p from S. cerevisiae has been crystallized by the hanging-drop method. A complete diffraction data set using synchrotron radiation was collected to 2.95  Å resolution.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1879-1881  [ doi:10.1107/S0907444902011022 ]

Crystallization and preliminary X-ray analysis of bucain, a novel toxin from the Malayan krait Bungarus candidus

L. Watanabe, S. Nirthanan, G. Rajaseger, I. Polikarpov, R. M. Kini and R. K. Arni

Synopsis: Crystallization of bucain, a three-finger toxin structurally homologous to snake-venom muscarin toxins, from the venom of the Malayan krait B. candidus is presented.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1882-1885  [ doi:10.1107/S0907444902013951 ]

Crystallization, X-ray characterization and selenomethionine phasing of Mlc1p bound to IQ motifs from myosin V

M. Terrak, L. R. Otterbein, G. Wu, L. A. Palecanda, R. C. Lu and R. Dominguez

Synopsis: Mlc1p is a myosin light chain that binds to IQ motifs of a class V myosin (Myo2p) and an IQGAP-like protein (Iqg1p), playing a role in cytokinesis and organelle transport in S. cerevisiae. Complexes of Mlc1p with IQ motifs 2, 3, 4, and 2,3 of Myo2p were crystallized and their structures determined.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1886-1888  [ doi:10.1107/S0907444902013318 ]

The use of construct variation and diffraction data analysis in the crystallization of the TRAF domain of human tumor necrosis factor receptor associated factor 6

H. Ye, M. Cirilli and H. Wu

Synopsis: Construct variation in conjunction with diffraction data analysis were used in the successful crystallization of the TRAF domain of TRAF6.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1889-1891  [ doi:10.1107/S0907444902012696 ]

Xtrack - a web-based crystallographic notebook

M. Harris and T. A. Jones

Synopsis: A web-based database-backed crystallographic notebook system is presented.

Online 28 September 2002

 

Acta Cryst. (2002). D58, 1892-1895  [ doi:10.1107/S0907444902013689 ]

A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a protein surface: external and internal AMPPNP molecules in crystalline N-acetyl-L-glutamate kinase

F. Gil-Ortiz, I. Fita, S. Ramón-Maiques, A. Marina and V. Rubio

Synopsis: A large volume of electron density in the crystal of Escherichia coli N-acetyl-L-glutamate kinase is interpreted as an external AMPPNP molecule that makes contacts with the enzyme through its -imidophosphate. This external nucleotide differs in a number of respects from the internal AMPPNP bound to the active site, and the possibility that the external AMPPNP is waiting to occupy the active center is discussed.

Online 28 September 2002