about
The 1.2 A resolution structure of the Con A-dimannose complexThe molecular basis of the coloration mechanism in lobster shell: beta-crustacyanin at 3.2-A resolutionApocrustacyanin C(1) crystals grown in space and on earth using vapour-diffusion geometry: protein structure refinements and electron-density map comparisonsCrystal structure of the C1 domain of cardiac myosin binding protein-C: implications for hypertrophic cardiomyopathyThe interdependence of wavelength, redundancy and dose in sulfur SAD experimentsCrystallographic analysis of counterion effects on subtilisin enzymatic action in acetonitrileRoom-temperature X-ray diffraction studies of cisplatin and carboplatin binding to His15 of HEWL after prolonged chemical exposureExperience with exchange and archiving of raw data: comparison of data from two diffractometers and four software packages on a series of lysozyme crystalsRaw diffraction data preservation and reuse: overview, update on practicalities and metadata requirements.Overview and new developments in softer X-ray (2A < lambda < 5A) protein crystallography.New leads for fragment-based design of rhenium/technetium radiopharmaceutical agents.Protein crystal perfection and its application.New opportunities in biological and chemical crystallography.Experiences with archived raw diffraction images data: capturing cisplatin after chemical conversion of carboplatin in high salt conditions for a protein crystal.Unravelling the structural chemistry of the colouration mechanism in lobster shell.Synchrotron and neutron techniques in biological crystallography.The combination of molecular dynamics with crystallography for elucidating protein-ligand interactions: a case study involving peanut lectin complexes with T-antigen and lactose.Active site of trypanothione reductase. A target for rational drug design.Improvements in lysozyme protein crystal perfection through microgravity growth.Diffraction structural biology - a new horizon.Roger Fourme (1942-2012).The structure and refinement of apocrustacyanin C2 to 1.3 A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1.The science is in the data.Principles and methods used to grow and optimize crystals of protein-metallodrug adducts, to determine metal binding sites and to assign metal ligands.The properties of (2Fo - Fc) and (Fo - Fc) electron-density maps at medium-to-high resolutions.High-resolution structures of single-metal-substituted concanavalin A: the Co,Ca-protein at 1.6 A and the Ni,Ca-protein at 2.0 A.Refined structure of concanavalin A complexed with methyl alpha-D-mannopyranoside at 2.0 A resolution and comparison with the saccharide-free structure.Report of the Working Group on Synchrotron Radiation Nomenclature - brightness, spectral brightness or brilliance?X-ray crystal structure and time-resolved spectroscopy of the blue carotenoid violerythrin.Crystallography: a down-to-Earth approach.S-SWAT (softer single-wavelength anomalous technique): potential in high-throughput protein crystallography.A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler.Interaction of counterions with subtilisin in acetonitrile: insights from molecular dynamics simulations.[14] Overview of synchrotron radiation and macromolecular crystallography.Crystallography and DatabasesChlamydia protein Pgp3 studied at high resolution in a new crystal formLight induced charge and energy transport in nucleic acids and proteins: general discussionLight induced damage and repair in nucleic acids and proteins: general discussionPhotocrosslinking between nucleic acids and proteins: general discussionInterdisciplinary research could pull cash into science
P50
Q27633215-F653D81A-BAC9-4FD5-A283-8CC748305024Q27639357-D6F8E6D1-DCC8-44C0-AA39-B52995825503Q27641520-B307F1EF-F68C-474D-9D01-4EDC88F2BA6BQ27650183-9130F333-B7FD-420C-8F0B-24D34BFE398AQ27652928-8E6EA8CB-2702-4366-85DF-BCB55F71330EQ27659164-66107267-74C2-4C20-8A6A-BC0CDA3E8A5EQ27675075-060C4035-370B-458F-A463-1B092F5DEBDBQ27676332-5CCDA602-97E9-40D3-80E3-F44CF40784DFQ27928081-C2BCD984-F5BF-480B-8212-6A5D54298B5CQ31029690-29DEB53D-7202-46C4-80EB-48A6D45F33E6Q33630722-BF378732-9C60-4887-98DB-07A1B1E92E19Q34423238-60E89AD9-690E-4DDB-9891-6F4EE792211EQ34486351-FACB6618-1D5C-4E13-ACDE-1C69BEFD3B9EQ35016386-77453C8E-B277-4349-8DE9-26DFB64651A4Q35596641-10ECC5C3-532D-47B5-9E4E-62D3BE200F26Q35916293-CC72F3E9-C964-4F33-B5A9-BC6D95D85C0CQ38295381-E6F6EE0A-A518-40EE-A223-B837AA44438DQ39088644-BBDA7B03-F498-4ED0-A3CC-957109B205B8Q40966114-1E9D1BAC-060E-42CD-B745-BA9B76EE88D7Q42668210-4B71CEF9-3F82-4377-9B5A-CCA3C6FD0620Q43530658-88C85A16-CAAE-4642-A6DA-62013CA517D1Q44782248-DD1A260B-F579-45DC-9465-52BF5ACEC83EQ46255967-C9011824-1CE3-4C09-B119-5ABE70CB3D7DQ47717493-9DDD27D2-533C-439D-982E-D1E20FBFA298Q47871942-4FDFA32E-0381-471F-BB0D-020103A900BFQ47985235-F3F4F81E-00F0-4996-AC50-7380308BC9CAQ47985328-16688CB7-1A81-4AE7-9E53-4A8F25F1C44AQ48710792-8C37EE5E-1F65-460D-9BE9-1363B73FFD24Q50444549-FFCFC274-92AE-413A-A249-A0C0A5F1EA55Q50939982-075BA56A-E049-446D-A648-7595D21BA7ECQ51293949-B816C8B5-E202-4D89-A329-D9299E0231CDQ51971118-F1BED68D-ACCF-4BA4-A4D6-FC6AC71570BBQ53099042-3548050E-9EBD-4FED-A04C-C0CB770DA215Q54038408-29205A01-538B-4BC4-BDAA-E341B5E44F4AQ56161323-1D0609E0-701B-41EE-83E0-5AB4296779FCQ56890718-D1537C92-4988-4E62-9591-7F3448CBD175Q59464087-E1029215-9EF1-4C39-9730-9551162B967DQ59464090-0AE80E8B-C2D3-4FF8-B045-3F5520E3E453Q59464092-D5820DD7-E64B-4F75-BE14-276710888BA9Q60097162-9B503D14-BF14-4CF7-8D42-F0723145ABAE
P50
description
hulumtues
@sq
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
name
John R. Helliwell
@ast
John R. Helliwell
@en
John R. Helliwell
@es
John R. Helliwell
@nl
John R. Helliwell
@sl
type
label
John R. Helliwell
@ast
John R. Helliwell
@en
John R. Helliwell
@es
John R. Helliwell
@nl
John R. Helliwell
@sl
altLabel
John Helliwell,John Richard Helliwell J R Helliwell
@en
prefLabel
John R. Helliwell
@ast
John R. Helliwell
@en
John R. Helliwell
@es
John R. Helliwell
@nl
John R. Helliwell
@sl
P1006
P214
P244
P1006
P1053
C-4587-2014
P106
P1153
8693358800
P21
P213
0000 0001 2418 1254
P214
P244
P31
P3829
P496
0000-0002-0520-7540
P734
P735
P7859
lccn-n91016067